Focus on Marine Animal Safety and Marine Bioresources in Response to the SARS-CoV-2 Crisis
Abstract
:1. Introduction
2. Genomic Structure of SARS-CoV-2 and Their Functions
2.1. Full Genetic Makeup of SARS-CoV-2
2.2. ORF1ab Cleavage
2.3. Structural Proteins
2.3.1. N Protein
2.3.2. E Protein
2.3.3. M Protein
2.3.4. S Protein
2.4. Accessory Proteins
2.5. Variants and Mutations
3. Threat to Marine Animals
4. Antiviral Activity against SARS-CoV-2 in Marine Resources
4.1. Targeting Viral Recognition and Interaction
4.1.1. Sulfated Polysaccharides
4.1.2. Inorganic Polyphosphates
4.1.3. Cyanobacteria Molecules
4.2. Targeting Viral Replication
4.2.1. Polyphenols against Mpro
4.2.2. Alkaloids against PLpro and Mpro
4.2.3. Plitidepsin against Host Factor eEF1A
5. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Sohrabi, C.; Alsafi, Z.; O’Neill, N.; Khan, M.; Kerwan, A.; Al-Jabir, A.; Iosifidis, C.; Agha, R. World Health Organization declares global emergency: A review of the 2019 novel coronavirus (COVID-19). Int. J. Surg. 2020, 76, 71–76. [Google Scholar] [CrossRef]
- Dhama, K.; Khan, S.; Tiwari, R.; Sircar, S.; Bhat, S.; Malik, Y.S.; Singh, K.P.; Chaicumpa, W.; Bonilla-Aldana, D.K.; Rodriguez-Morales, A.J. Coronavirus Disease 2019-COVID-19. Clin. Microbiol. Rev. 2020, 33, e00028-20. [Google Scholar] [CrossRef] [PubMed]
- Cucinotta, D.; Vanelli, M. WHO Declares COVID-19 a Pandemic. Acta Biomed. 2020, 91, 157–160. [Google Scholar]
- Fehr, A.R.; Perlman, S. Coronaviruses: An overview of their replication and pathogenesis. Methods Mol. Biol. 2015, 1282, 1–23. [Google Scholar]
- Paim, F.C.; Bowman, A.S.; Miller, L.; Feehan, B.J.; Marthaler, D.; Saif, L.J.; Vlasova, A.N. Epidemiology of deltacoronaviruses (δ-CoV) and gammacoronaviruses (γ-CoV) in wild birds in the United States. Viruses 2019, 11, 897. [Google Scholar] [CrossRef] [Green Version]
- Letko, M.; Marzi, A.; Munster, V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat. Microbiol. 2020, 5, 562–569. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wu, F.; Zhao, S.; Yu, B.; Chen, Y.M.; Wang, W.; Song, Z.G.; Hu, Y.; Tao, Z.W.; Tian, J.H.; Pei, Y.Y.; et al. A new coronavirus associated with human respiratory disease in China. Nature 2020, 579, 265–269. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kim, D.; Lee, J.Y.; Yang, J.S.; Kim, J.W.; Kim, V.N.; Chang, H. The Architecture of SARS-CoV-2 transcriptome. Cell 2020, 181, 914–921.e10. [Google Scholar] [CrossRef]
- Jungreis, I.; Sealfon, R.; Kellis, M. SARS-CoV-2 gene content and COVID-19 mutation impact by comparing 44 Sarbecovirus genomes. Nat. Commun. 2021, 12, 2642. [Google Scholar] [CrossRef]
- Jungreis, I.; Nelson, C.W.; Ardern, Z.; Finkel, Y.; Krogan, N.J.; Sato, K.; Ziebuhr, J.; Stern-Ginossar, N.; Pavesi, A.; Firth, A.E.; et al. Conflicting and ambiguous names of overlapping ORFs in the SARS-CoV-2 genome: A homology-based resolution. Virology 2021, 558, 145–151. [Google Scholar] [CrossRef]
- Lu, R.; Zhao, X.; Li, J.; Niu, P.; Yang, B.; Wu, H.; Wang, W.; Song, H.; Huang, B.; Zhu, N.; et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: Implications for virus origins and receptor binding. Lancet 2020, 395, 565–574. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Koev, G.; Miller, W.A. A positive-strand RNA virus with three very different subgenomic RNA promoters. J. Virol. 2000, 74, 5988–5996. [Google Scholar] [CrossRef]
- Brant, A.C.; Tian, W.; Majerciak, V.; Yang, W.; Zheng, Z.M. SARS-CoV-2: From its discovery to genome structure, transcription, and replication. Cell Biosci. 2021, 11, 136. [Google Scholar] [CrossRef]
- Long, S. SARS-CoV-2 Subgenomic RNAs: Characterization, Utility, and Perspectives. Viruses 2021, 13, 1923. [Google Scholar] [CrossRef]
- Slanina, H.; Madhugiri, R.; Bylapudi, G.; Schultheiß, K.; Karl, N.; Gulyaeva, A.; Gorbalenya, A.E.; Linne, U.; Ziebuhr, J. Coronavirus replication–transcription complex: Vital and selective NMPylation of a conserved site in nsp9 by the NiRAN-RdRp subunit. Proc. Natl. Acad. Sci. USA 2021, 118, e2022310118. [Google Scholar] [CrossRef] [PubMed]
- Mariano, G.; Farthing, R.J.; Lale-Farjat, S.L.M.; Bergeron, J.R.C. Structural characterization of SARS-CoV-2: Where we are, and where we need to be. Front. Mol. Biosci. 2020, 7, 605236. [Google Scholar] [CrossRef] [PubMed]
- Kelly, J.A.; Woodside, M.T.; Dinman, J.D. Programmed-1 Ribosomal Frameshifting in coronaviruses: A therapeutic target. Virology 2021, 554, 75–82. [Google Scholar] [CrossRef] [PubMed]
- Chan, J.F.; Kok, K.H.; Zhu, Z.; Chu, H.; To, K.K.; Yuan, S.; Yuen, K.Y. Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan. Emerg. Microbes Infect. 2020, 9, 221–236. [Google Scholar] [CrossRef] [Green Version]
- Osipiuk, J.; Azizi, S.-A.; Dvorkin, S.; Endres, M.; Jedrzejczak, R.; Jones, K.A.; Kang, S.; Kathayat, R.S.; Kim, Y.; Lisnyak, V.G.; et al. Structure of papain-like protease from SARS-CoV-2 and its complexes with non-covalent inhibitors. Nat. Commun. 2021, 12, 743. [Google Scholar] [CrossRef]
- Schubert, K.; Karousis, E.D.; Jomaa, A.; Scaiola, A.; Echeverria, B.; Gurzeler, L.A.; Leibundgut, M.; Thiel, V.; Mühlemann, O.; Ban, N. SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. Nat. Struct. Mol. Biol. 2020, 27, 959–966. [Google Scholar] [CrossRef]
- Mendez, A.S.; Ly, M.; González-Sánchez, A.M.; Hartenian, E.; Ingolia, N.T.; Cate, J.H.; Glaunsinger, B.A. The N-terminal domain of SARS-CoV-2 nsp1 plays key roles in suppression of cellular gene expression and preservation of viral gene expression. Cell Rep. 2021, 37, 109841. [Google Scholar] [CrossRef] [PubMed]
- Zou, L.; Moch, C.; Graille, M.; Chapat, C. The SARS-CoV-2 protein NSP2 impairs the silencing capacity of the human 4EHP-GIGYF2 complex. iScience 2022, 25, 104646. [Google Scholar] [CrossRef] [PubMed]
- Shi, R.; Feng, Z.; Zhang, X. Integrative multi-omics landscape of non-structural protein 3 of severe acute respiratory syndrome coronaviruses. Genom. Proteom. Bioinform. 2021, 19, 707–726. [Google Scholar] [CrossRef] [PubMed]
- Konkolova, E.; Klima, M.; Nencka, R.; Boura, E. Structural analysis of the putative SARS-CoV-2 primase complex. J. Struct. Biol. 2020, 211, 107548. [Google Scholar] [CrossRef] [PubMed]
- Chen, J.; Malone, B.; Llewellyn, E.; Grasso, M.; Shelton, P.M.M.; Olinares, P.D.B.; Maruthi, K.; Eng, E.T.; Vatandaslar, H.; Chait, B.T.; et al. Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex. Cell 2020, 182, 1560–1573.e13. [Google Scholar] [CrossRef] [PubMed]
- Moeller, N.H.; Shi, K.; Demir, Ö.; Belica, C.; Banerjee, S.; Yin, L.; Durfee, C.; Amaro, R.E.; Aihara, H. Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN. Proc. Natl. Acad. Sci. USA 2022, 119, e2106379119. [Google Scholar] [CrossRef]
- Benoni, R.; Krafcikova, P.; Baranowski, M.R.; Kowalska, J.; Boura, E.; Cahová, H. Substrate specificity of SARS-CoV-2 nsp10-nsp16 methyltransferase. Viruses 2021, 13, 1722. [Google Scholar] [CrossRef] [PubMed]
- Guo, G.; Gao, M.; Gao, X.; Zhu, B.; Huang, J.; Luo, K.; Zhang, Y.; Sun, J.; Deng, M.; Lou, Z. SARS-CoV-2 non-structural protein 13 (nsp13) hijacks host deubiquitinase USP13 and counteracts host antiviral immune response. Signal Transduct. Target. Ther. 2021, 6, 119. [Google Scholar] [CrossRef]
- Jahirul Islam, M.; Nawal Islam, N.; Siddik Alom, M.; Kabir, M.; Halim, M.A. A Review on structural, non-structural, and accessory proteins of SARS-CoV-2: Highlighting drug target sites. Immunobiology 2022, 228, 152302. [Google Scholar] [CrossRef] [PubMed]
- Lu, S.; Ye, Q.; Singh, D.; Villa, E.; Cleveland, D.W.; Corbett, K.D. The SARS-CoV-2 Nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein. Nat. Commun. 2020, 12, 502. [Google Scholar] [CrossRef]
- Cubuk, J.; Alston, J.J.; Incicco, J.J.; Singh, S.; Stuchell-Brereton, M.D.; Ward, M.D.; Zimmerman, M.I.; Vithani, N.; Griffith, D.; Wagoner, J.A.; et al. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. Nat. Commun. 2021, 12, 1936. [Google Scholar] [CrossRef] [PubMed]
- Iserman, C.; Roden, C.A.; Boerneke, M.A.; Sealfon, R.S.G.; McLaughlin, G.A.; Jungreis, I.; Fritch, E.J.; Hou, Y.J.; Ekena, J.; Weidmann, C.A.; et al. Genomic RNA elements drive phase separation of the SARS-CoV-2 nucleocapsid. Mol. Cell 2020, 80, 1078–1091.e6. [Google Scholar] [CrossRef] [PubMed]
- Perdikari, T.M.; Murthy, A.C.; Ryan, V.H.; Watters, S.; Naik, M.T.; Fawzi, N.L. SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs. EMBO J. 2020, 39, e106478. [Google Scholar] [CrossRef]
- Syed, A.M.; Taha, T.Y.; Tabata, T.; Chen, I.P.; Ciling, A.; Khalid, M.M.; Sreekumar, B.; Chen, P.Y.; Hayashi, J.M.; Soczek, K.M.; et al. Rapid assessment of SARS-CoV-2-evolved variants using virus-like particles. Science 2021, 374, 1626–1632. [Google Scholar] [CrossRef]
- Cao, Y.; Yang, R.; Lee, I.; Zhang, W.; Sun, J.; Wang, W.; Meng, X. Characterization of the SARS-CoV-2 E protein: Sequence, structure, viroporin, and inhibitors. Protein Sci. 2021, 30, 1114–1130. [Google Scholar] [CrossRef]
- Kuzmin, A.; Orekhov, P.; Astashkin, R.; Gordeliy, V.; Gushchin, I. Structure and dynamics of the SARS-CoV-2 envelope protein monomer. Proteins 2022, 90, 1102–1114. [Google Scholar] [CrossRef]
- Zhang, Z.; Nomura, N.; Muramoto, Y.; Ekimoto, T.; Uemura, T.; Liu, K.; Yui, M.; Kono, N.; Aoki, J.; Ikeguchi, M.; et al. Structure of SARS-CoV-2 membrane protein essential for virus assembly. Nat. Commun. 2022, 13, 4399. [Google Scholar] [CrossRef] [PubMed]
- Kumar, P.; Kumar, A.; Garg, N.; Giri, R. An insight into SARS-CoV-2 membrane protein interaction with spike, envelope, and nucleocapsid proteins. J. BioMol. Struct. Dyn. 2021, 1–10. [Google Scholar] [CrossRef] [PubMed]
- Zhang, J.; Xiao, T.; Cai, Y.; Chen, B. Structure of SARS-CoV-2 spike protein. Curr. Opin. Virol. 2021, 50, 173–182. [Google Scholar] [CrossRef] [PubMed]
- Jackson, C.B.; Farzan, M.; Chen, B.; Choe, H. Mechanisms of SARS-CoV-2 entry into cells. Nat. Rev. Mol. Cell Biol. 2022, 23, 3–20. [Google Scholar] [CrossRef] [PubMed]
- Ou, X.; Liu, Y.; Lei, X.; Li, P.; Mi, D.; Ren, L.; Guo, L.; Guo, R.; Chen, T.; Hu, J.; et al. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV. Nat. Commun. 2020, 11, 1620. [Google Scholar] [CrossRef] [Green Version]
- Shang, J.; Wan, Y.; Luo, C.; Ye, G.; Geng, Q.; Auerbach, A.; Li, F. Cell entry mechanisms of SARS-CoV-2. Proc. Natl. Acad. Sci. USA 2020, 117, 11727–11734. [Google Scholar] [CrossRef] [PubMed]
- Papa, G.; Mallery, D.L.; Albecka, A.; Welch, L.G.; Cattin-Ortolá, J.; Luptak, J.; Paul, D.; McMahon, H.T.; Goodfellow, I.G.; Carter, A.; et al. Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion. PLoS Pathog. 2021, 17, e1009246. [Google Scholar] [CrossRef]
- Henderson, R.; Edwards, R.J.; Mansouri, K.; Janowska, K.; Stalls, V.; Gobeil, S.M.C.; Kopp, M.; Li, D.; Parks, R.; Hsu, A.L.; et al. Controlling the SARS-CoV-2 spike glycoprotein conformation. Nat. Struct. Mol. Biol. 2020, 27, 925–933. [Google Scholar] [CrossRef] [PubMed]
- Bestle, D.; Heindl, M.R.; Limburg, H.; Van Lam van, T.; Pilgram, O.; Moulton, H.; Stein, D.A.; Hardes, K.; Eickmann, M.; Dolnik, O.; et al. TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells. Life Sci. Alliance 2020, 3, e202000786. [Google Scholar] [CrossRef] [PubMed]
- Icho, S.; Rujas, E.; Muthuraman, K.; Tam, J.; Liang, H.; Landreth, S.; Liao, M.; Falzarano, D.; Julien, J.P.; Melnyk, R.A. Dual inhibition of vacuolar-ATPase and TMPRSS2 is required for complete blockade of SARS-CoV-2 entry into cells. Antimicrob. Agents Chemother. 2022, 66, e0043922. [Google Scholar] [CrossRef] [PubMed]
- Shah, P.; Canziani, G.A.; Carter, E.P.; Chaiken, I. The case for S2: The potential benefits of the S2 subunit of the SARS-CoV-2 spike protein as an immunogen in fighting the COVID-19 pandemic. Front. Immunol. 2021, 12, 637651. [Google Scholar] [CrossRef]
- Jin, S.; He, X.; Ma, L.; Zhuang, Z.; Wang, Y.; Lin, M.; Cai, S.; Wei, L.; Wang, Z.; Zhao, Z.; et al. Suppression of ACE2 SUMOylation protects against SARS-CoV-2 infection through TOLLIP-mediated selective autophagy. Nat. Commun. 2022, 13, 5204. [Google Scholar] [CrossRef]
- Redondo, N.; Zaldívar-López, S.; Garrido, J.J.; Montoya, M. SARS-CoV-2 accessory proteins in viral pathogenesis: Knowns and unknowns. Front. Immunol. 2021, 12, 708264. [Google Scholar] [CrossRef]
- Hayn, M.; Hirschenberger, M.; Koepke, L.; Nchioua, R.; Straub, J.H.; Klute, S.; Hunszinger, V.; Zech, F.; Prelli Bozzo, C.; Aftab, W.; et al. Systematic functional analysis of SARS-CoV-2 proteins uncovers viral innate immune antagonists and remaining vulnerabilities. Cell Rep. 2021, 35, 109126. [Google Scholar] [CrossRef]
- Ren, Y.; Shu, T.; Wu, D.; Mu, J.; Wang, C.; Huang, M.; Han, Y.; Zhang, X.Y.; Zhou, W.; Qiu, Y.; et al. The ORF3a protein of SARS-CoV-2 induces apoptosis in cells. Cell Mol. Immunol. 2020, 17, 881–883. [Google Scholar] [CrossRef] [PubMed]
- Silvas, J.A.; Vasquez, D.M.; Park, J.G.; Chiem, K.; Allué-Guardia, A.; Garcia-Vilanova, A.; Platt, R.N.; Miorin, L.; Kehrer, T.; Cupic, A.; et al. Contribution of SARS-CoV-2 accessory proteins to viral pathogenicity in K18 human ACE2 transgenic mice. J. Virol. 2021, 95, e0040221. [Google Scholar] [CrossRef] [PubMed]
- Li, J.Y.; Liao, C.H.; Wang, Q.; Tan, Y.J.; Luo, R.; Qiu, Y.; Ge, X.Y. The ORF6, ORF8 and nucleocapsid proteins of SARS-CoV-2 inhibit type I interferon signaling pathway. Virus Res. 2020, 286, 198074. [Google Scholar] [CrossRef] [PubMed]
- Yang, R.; Zhao, Q.; Rao, J.; Zeng, F.; Yuan, S.; Ji, M.; Sun, X.; Li, J.; Yang, J.; Cui, J.; et al. SARS-CoV-2 Accessory protein ORF7b mediates tumor necrosis factor-α-induced apoptosis in cells. Front. Microbiol. 2021, 12, 654709. [Google Scholar] [CrossRef] [PubMed]
- Gordon, D.E.; Hiatt, J.; Bouhaddou, M.; Rezelj, V.V.; Ulferts, S.; Braberg, H.; Jureka, A.S.; Obernier, K.; Guo, J.Z.; Batra, J.; et al. Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms. Science 2020, 370, eabe9403. [Google Scholar] [CrossRef] [PubMed]
- Gao, X.; Zhu, K.; Qin, B.; Olieric, V.; Wang, M.; Cui, S. Crystal structure of SARS-CoV-2 Orf9b in complex with human TOM70 suggests unusual virus-host interactions. Nat. Commun. 2021, 12, 2843. [Google Scholar] [CrossRef]
- Lin, R.; Paz, S.; Hiscott, J. Tom70 imports antiviral immunity to the mitochondria. Cell Res. 2010, 20, 971–973. [Google Scholar] [CrossRef] [PubMed]
- Eskier, D.; Suner, A.; Oktay, Y.; Karakülah, G. Mutations of SARS-CoV-2 nsp14 exhibit strong association with increased genome-wide mutation load. PeerJ 2020, 8, e10181. [Google Scholar] [CrossRef] [PubMed]
- McCarthy, K.R.; Rennick, L.J.; Nambulli, S.; Robinson-McCarthy, L.R.; Bain, W.G.; Haidar, G.; Duprex, W.P. Recurrent deletions in the SARS-CoV-2 spike glycoprotein drive antibody escape. Science 2021, 371, 1139–1142. [Google Scholar] [CrossRef]
- Willett, B.J.; Grove, J.; MacLean, O.A.; Wilkie, C.; De Lorenzo, G.; Furnon, W.; Cantoni, D.; Scott, S.; Logan, N.; Ashraf, S.; et al. SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway. Nat. Microbiol. 2022, 7, 1161–1179. [Google Scholar] [CrossRef] [PubMed]
- SARS-CoV-2 (hCoV-19) Mutation Reports. Available online: https://outbreak.info/situation-reports/omicron (accessed on 15 November 2022).
- Barton, M.I.; MacGowan, S.A.; Kutuzov, M.A.; Dushek, O.; Barton, G.J.; van der Merwe, P.A. Effects of common mutations in the SARS-CoV-2 Spike RBD and its ligand, the human ACE2 receptor on binding affinity and kinetics. eLife 2021, 10, e70658. [Google Scholar] [CrossRef] [PubMed]
- Lubinski, B.; Fernandes, M.H.V.; Frazier, L.; Tang, T.; Daniel, S.; Diel, D.G.; Jaimes, J.A.; Whittaker, G.R. Functional evaluation of the P681H mutation on the proteolytic activation of the SARS-CoV-2 variant B.1.1.7 (Alpha) spike. iScience 2022, 25, 103589. [Google Scholar] [CrossRef] [PubMed]
- Abdel-Moneim, A.S.; Abdelwhab, E.M. Evidence for SARS-CoV-2 Infection of Animal Hosts. Pathogens 2020, 9, 529. [Google Scholar] [CrossRef]
- SARS-CoV-2 in Animals—Situation Report 15. Available online: https://www.woah.org/en/document/86934/ (accessed on 6 November 2022).
- Gryseels, S.; De Bruyn, L.; Gyselings, R.; Calvignac-Spencer, S.; Leendertz, F.H.; Leirs, H. Risk of human-to-wildlife transmission of SARS-CoV-2. Mamm. Rev. 2021, 51, 272–292. [Google Scholar] [CrossRef]
- Tan, C.C.S.; Lam, S.D.; Richard, D.; Owen, C.J.; Berchtold, D.; Orengo, C.; Nair, M.S.; Kuchipudi, S.V.; Kapur, V.; van Dorp, L.; et al. Transmission of SARS-CoV-2 from humans to animals and potential host adaptation. Nat. Commun. 2022, 13, 2988. [Google Scholar] [CrossRef] [PubMed]
- Karthikeyan, S.; Levy, J.I.; De Hoff, P.; Humphrey, G.; Birmingham, A.; Jepsen, K.; Farmer, S.; Tubb, H.M.; Valles, T.; Tribelhorn, C.E.; et al. Wastewater sequencing reveals early cryptic SARS-CoV-2 variant transmission. Nature 2022, 609, 101–108. [Google Scholar] [CrossRef] [PubMed]
- Tran, H.N.; Le, G.T.; Nguyen, D.T.; Juang, R.S.; Rinklebe, J.; Bhatnagar, A.; Lima, E.C.; Iqbal, H.M.N.; Sarmah, A.K.; Chao, H.P. SARS-CoV-2 coronavirus in water and wastewater: A critical review about presence and concern. Environ. Res. 2021, 193, 110265. [Google Scholar] [CrossRef]
- Zhang, F.; Li, Z.; Yin, L.; Zhang, Q.; Askarinam, N.; Mundaca-Uribe, R.; Tehrani, F.; Karshalev, E.; Gao, W.; Zhang, L.; et al. ACE2 receptor-modified algae-based microrobot for removal of SARS-CoV-2 in wastewater. J. Am. Chem. Soc. 2021, 143, 12194–12201. [Google Scholar] [CrossRef] [PubMed]
- Desdouits, M.; Piquet, J.C.; Wacrenier, C.; Le Mennec, C.; Parnaudeau, S.; Jousse, S.; Rocq, S.; Bigault, L.; Contrant, M.; Garry, P.; et al. Can shellfish be used to monitor SARS-CoV-2 in the coastal environment? Sci. Total Environ. 2021, 778, 146270. [Google Scholar] [CrossRef] [PubMed]
- Polo, D.; Lois, M.; Fernández-Núñez, M.T.; Romalde, J.L. Detection of SARS-CoV-2 RNA in bivalve mollusks and marine sediments. Sci. Total Environ. 2021, 786, 147534. [Google Scholar] [CrossRef]
- Seyer, A. The fate of SARS-CoV-2 in the marine environments: Are marine environments safe of COVID-19? Erciyes Med. J. 2021, 43, 606–607. [Google Scholar]
- Mordecai, G.J.; Miller, K.M.; Di Cicco, E.; Schulze, A.D.; Kaukinen, K.H.; Ming, T.J.; Li, S.; Tabata, A.; Teffer, A.; Patterson, D.A.; et al. Endangered wild salmon infected by newly discovered viruses. eLife 2019, 8, e47615. [Google Scholar] [CrossRef] [PubMed]
- Johnstone, C.; Báez, J.C. Placing the COVID-19 Pandemic in a Marine Ecological Context: Potential risks for conservation of marine air-breathing animals and future zoonotic outbreaks. Front. Mar. Sci. 2021, 8, 691682. [Google Scholar] [CrossRef]
- Barbosa, A.; Varsani, A.; Morandini, V.; Grimaldi, W.; Vanstreels, R.E.T.; Diaz, J.I.; Boulinier, T.; Dewar, M.; González-Acuña, D.; Gray, R.; et al. Risk assessment of SARS-CoV-2 in Antarctic wildlife. Sci. Total Environ. 2021, 755, 143352. [Google Scholar] [CrossRef]
- Damas, J.; Hughes, G.M.; Keough, K.C.; Painter, C.A.; Persky, N.S.; Corbo, M.; Hiller, M.; Koepfli, K.-P.; Pfenning, A.R.; Zhao, H.; et al. Broad host range of SARS-CoV-2 predicted by comparative and structural analysis of ACE2 in vertebrates. Proc. Natl. Acad. Sci. USA 2020, 117, 22311–22322. [Google Scholar] [CrossRef] [PubMed]
- Mathavarajah, S.; Stoddart, A.K.; Gagnon, G.A.; Dellaire, G. Pandemic danger to the deep: The risk of marine mammals contracting SARS-CoV-2 from wastewater. Sci. Total Environ. 2021, 760, 143346. [Google Scholar] [CrossRef] [PubMed]
- Audino, T.; Grattarola, C.; Centelleghe, C.; Peletto, S.; Giorda, F.; Florio, C.L.; Caramelli, M.; Bozzetta, E.; Mazzariol, S.; Di Guardo, G.; et al. SARS-CoV-2, a threat to marine mammals? A study from Italian seawaters. Animals 2021, 11, 1663. [Google Scholar] [CrossRef]
- Xie, S.Z.; Liu, M.Q.; Jiang, R.D.; Lin, H.F.; Zhang, W.; Li, B.; Su, J.; Ke, F.; Zhang, Q.Y.; Shi, Z.L.; et al. Fish ACE2 is not susceptible to SARS-CoV-2. Virol. Sin. 2022, 37, 142–144. [Google Scholar] [CrossRef] [PubMed]
- Patel, R.; Kaki, M.; Potluri, V.S.; Kahar, P.; Khanna, D. A comprehensive review of SARS-CoV-2 vaccines: Pfizer, Moderna & Johnson & Johnson. Hum. Vaccines Immunother. 2022, 18, 2002083. [Google Scholar]
- Gobeil, P.; Pillet, S.; Boulay, I.; Charland, N.; Lorin, A.; Cheng, M.P.; Vinh, D.C.; Boutet, P.; Van Der Most, R.; Roman, F.; et al. Durability and cross-reactivity of immune responses induced by a plant-based virus-like particle vaccine for COVID-19. Nat. Commun. 2022, 13, 6905. [Google Scholar] [CrossRef] [PubMed]
- Lipsitch, M.; Krammer, F.; Regev-Yochay, G.; Lustig, Y.; Balicer, R.D. SARS-CoV-2 breakthrough infections in vaccinated individuals: Measurement, causes and impact. Nat. Rev. Immunol. 2022, 22, 57–65. [Google Scholar] [CrossRef] [PubMed]
- Götte, M. Remdesivir for the treatment of COVID-19: The value of biochemical studies. Curr. Opin. Virol. 2021, 49, 81–85. [Google Scholar] [CrossRef]
- Iglesias Gómez, R.; Méndez, R.; Palanques-Pastor, T.; Ballesta-López, O.; Borrás Almenar, C.; Megías Vericat, J.E.; López-Briz, E.; Font-Noguera, I.; Menéndez Villanueva, R.; Román Iborra, J.A.; et al. Baricitinib against severe COVID-19: Effectiveness and safety in hospitalised pretreated patients. Eur. J. Hosp. Pharm. 2022, 29, e41–e45. [Google Scholar] [CrossRef] [PubMed]
- Titanji, B.K.; Farley, M.M.; Mehta, A.; Connor-Schuler, R.; Moanna, A.; Cribbs, S.K.; O’Shea, J.; DeSilva, K.; Chan, B.; Edwards, A.; et al. Use of baricitinib in patients with moderate to severe coronavirus disease 2019. Clin. Infect. Dis. 2021, 72, 1247–1250. [Google Scholar] [CrossRef] [PubMed]
- Liu, Y.; Gan, J.; Wang, R.; Yang, X.; Xiao, Z.; Cao, Y. DrugDevCovid19: An atlas of anti-COVID-19 compounds derived by computer-aided drug design. Molecules 2022, 27, 683. [Google Scholar] [CrossRef] [PubMed]
- Peng, H.; Ding, C.; Jiang, L.; Tang, W.; Liu, Y.; Zhao, L.; Yi, Z.; Ren, H.; Li, C.; He, Y.; et al. Discovery of potential anti-SARS-CoV-2 drugs based on large-scale screening in vitro and effect evaluation in vivo. Sci. China Life Sci. 2022, 65, 1181–1197. [Google Scholar] [CrossRef] [PubMed]
- Kim, C.-H. Anti–SARS-CoV-2 natural products as potentially therapeutic agents. Front. Pharmacol. 2021, 12, 590509. [Google Scholar] [CrossRef]
- Rahman, M.M.; Islam, M.R.; Shohag, S.; Hossain, M.E.; Shah, M.; Shuvo, S.K.; Khan, H.; Chowdhury, M.A.R.; Bulbul, I.J.; Hossain, M.S.; et al. Multifaceted role of natural sources for COVID-19 pandemic as marine drugs. Environ. Sci. Pollut. Res. Int. 2022, 29, 46527–46550. [Google Scholar] [CrossRef] [PubMed]
- Andrew, M.; Jayaraman, G. Marine sulfated polysaccharides as potential antiviral drug candidates to treat Corona Virus disease (COVID-19). Carbohydr. Res. 2021, 505, 108326. [Google Scholar] [CrossRef] [PubMed]
- Neufurth, M.; Wang, X.; Tolba, E.; Lieberwirth, I.; Wang, S.; Schröder, H.C.; Müller, W.E.G. The inorganic polymer, polyphosphate, blocks binding of SARS-CoV-2 spike protein to ACE2 receptor at physiological concentrations. Biochem. Pharmacol. 2020, 182, 114215. [Google Scholar] [CrossRef]
- Müller, W.E.G.; Neufurth, M.; Schepler, H.; Wang, S.; Tolba, E.; Schröder, H.C.; Wang, X. The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor. Biomater. Sci. 2020, 8, 6603–6610. [Google Scholar] [CrossRef]
- Petit, L.; Vernès, L.; Cadoret, J.P. Docking and in silico toxicity assessment of Arthrospira compounds as potential antiviral agents against SARS-CoV-2. J. Appl. Phycol. 2021, 33, 1579–1602. [Google Scholar] [CrossRef] [PubMed]
- Barre, A.; Van Damme, E.J.M.; Simplicien, M.; Le Poder, S.; Klonjkowski, B.; Benoist, H.; Peyrade, D.; Rougé, P. Man-specific lectins from plants, fungi, algae and cyanobacteria, as potential blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) coronaviruses: Biomedical perspectives. Cells 2021, 10, 1619. [Google Scholar] [CrossRef] [PubMed]
- Arunkumar, M.; Gunaseelan, S.; Kubendran Aravind, M.; Mohankumar, V.; Anupam, P.; Harikrishnan, M.; Siva, A.; Ashokkumar, B.; Varalakshmi, P. Marine algal antagonists targeting 3CL protease and spike glycoprotein of SARS-CoV-2: A computational approach for anti-COVID-19 drug discovery. J. BioMol. Struct. Dyn. 2021, 1–28. [Google Scholar] [CrossRef] [PubMed]
- Gentile, D.; Patamia, V.; Scala, A.; Sciortino, M.T.; Piperno, A.; Rescifina, A. Putative inhibitors of SARS-CoV-2 main protease from a library of marine natural products: A virtual screening and molecular modeling study. Mar. Drugs 2020, 18, 225. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- El-Demerdash, A.; Metwaly, A.M.; Hassan, A.; Abd El-Aziz, T.M.; Elkaeed, E.B.; Eissa, I.H.; Arafa, R.K.; Stockand, J.D. Comprehensive virtual screening of the antiviral potentialities of marine polycyclic guanidine alkaloids against SARS-CoV-2 (COVID-19). Biomolecules 2021, 11, 460. [Google Scholar] [CrossRef] [PubMed]
- Khan, M.T.; Ali, A.; Wang, Q.; Irfan, M.; Khan, A.; Zeb, M.T.; Zhang, Y.J.; Chinnasamy, S.; Wei, D.Q. Marine natural compounds as potents inhibitors against the main protease of SARS-CoV-2-a molecular dynamic study. J. BioMol. Struct. Dyn. 2021, 39, 3627–3637. [Google Scholar] [CrossRef]
- Quimque, M.T.J.; Notarte, K.I.R.; Fernandez, R.A.T.; Mendoza, M.A.O.; Liman, R.A.D.; Lim, J.A.K.; Pilapil, L.A.E.; Ong, J.K.H.; Pastrana, A.M.; Khan, A.; et al. Virtual screening-driven drug discovery of SARS-CoV2 enzyme inhibitors targeting viral attachment, replication, post-translational modification and host immunity evasion infection mechanisms. J. BioMol. Struct. Dyn. 2021, 39, 4316–4333. [Google Scholar] [CrossRef] [PubMed]
- Abdelrheem, D.A.; Ahmed, S.A.; Abd El-Mageed, H.R.; Mohamed, H.S.; Rahman, A.A.; Elsayed, K.N.M.; Ahmed, S.A. The inhibitory effect of some natural bioactive compounds against SARS-CoV-2 main protease: Insights from molecular docking analysis and molecular dynamic simulation. J. Environ. Sci. Health A Toxic Hazard. Subst. Environ. Eng. 2020, 55, 1373–1386. [Google Scholar] [CrossRef]
- Pendyala, B.; Patras, A.; Dash, C. Phycobilins as potent food bioactive broad-spectrum inhibitors against proteases of SARS-CoV-2 and other coronaviruses: A preliminary study. Front. Microbiol. 2021, 12, 645713. [Google Scholar] [CrossRef] [PubMed]
- Vijayaraj, R.; Altaff, K.; Rosita, A.S.; Ramadevi, S.; Revathy, J. Bioactive compounds from marine resources against novel corona virus (2019-nCoV): In silico study for corona viral drug. Nat. Prod. Res. 2021, 35, 5525–5529. [Google Scholar] [CrossRef] [PubMed]
- Bhati, S. Structure-based drug designing of naphthalene based SARS-CoV PLpro inhibitors for the treatment of COVID-19. Heliyon 2020, 6, e05558. [Google Scholar] [CrossRef]
- Hamoda, A.M.; Fayed, B.; Ashmawy, N.S.; El-Shorbagi, A.A.; Hamdy, R.; Soliman, S.S.M. Marine sponge is a promising natural source of anti-SARS-CoV-2 scaffold. Front. Pharmacol. 2021, 12, 666664. [Google Scholar] [CrossRef] [PubMed]
- Mahmudpour, M.; Nabipour, I.; Keshavarz, M.; Farrokhnia, M. Virtual screening on marine natural products for discovering TMPRSS2 inhibitors. Front. Chem. 2021, 9, 722633. [Google Scholar] [CrossRef] [PubMed]
- Ferrucci, V.; Kong, D.Y.; Asadzadeh, F.; Marrone, L.; Boccia, A.; Siciliano, R.; Criscuolo, G.; Anastasio, C.; Quarantelli, F.; Comegna, M.; et al. Long-chain polyphosphates impair SARS-CoV-2 infection and replication. Sci. Signal 2021, 14, eabe5040. [Google Scholar] [CrossRef] [PubMed]
- Sahu, N.; Mishra, S.; Kesheri, M.; Kanchan, S.; Sinha, R.P. Identification of cyanobacteria-based natural inhibitors against SARS-CoV-2 druggable target ACE2 using molecular docking study, ADME and toxicity analysis. Indian J. Clin. Biochem. 2022, 1–13. [Google Scholar] [CrossRef] [PubMed]
- Müller, W.E.G.; Neufurth, M.; Wang, S.; Tan, R.; Schröder, H.C.; Wang, X. Morphogenetic (mucin expression) as well as potential anti-corona viral activity of the marine secondary metabolite polyphosphate on A549 cells. Mar. Drugs 2020, 18, 639. [Google Scholar] [CrossRef] [PubMed]
- Leisch, M.; Egle, A.; Greil, R. Plitidepsin: A potential new treatment for relapsed/refractory multiple myeloma. Future Oncol. 2019, 15, 109–120. [Google Scholar] [CrossRef]
- White, K.M.; Rosales, R.; Yildiz, S.; Kehrer, T.; Miorin, L.; Moreno, E.; Jangra, S.; Uccellini, M.B.; Rathnasinghe, R.; Coughlan, L.; et al. Plitidepsin has potent preclinical efficacy against SARS-CoV-2 by targeting the host protein eEF1A. Science 2021, 371, 926–931. [Google Scholar] [CrossRef]
- Xie, Y.; Karki, C.B.; Du, D.; Li, H.; Wang, J.; Sobitan, A.; Teng, S.; Tang, Q.; Li, L. Spike proteins of SARS-CoV and SARS-CoV-2 utilize different mechanisms to bind with human ACE2. Front. Mol. Biosci. 2020, 7, 392. [Google Scholar] [CrossRef]
- Song, S.; Peng, H.; Wang, Q.; Liu, Z.; Dong, X.; Wen, C.; Ai, C.; Zhang, Y.; Wang, Z.; Zhu, B. Inhibitory activities of marine sulfated polysaccharides against SARS-CoV-2. Food Funct. 2020, 11, 7415–7420. [Google Scholar] [CrossRef] [PubMed]
- Schütz, D.; Conzelmann, C.; Fois, G.; Groß, R.; Weil, T.; Wettstein, L.; Stenger, S.; Zelikin, A.; Hoffmann, T.K.; Frick, M.; et al. Carrageenan-containing over-the-counter nasal and oral sprays inhibit SARS-CoV-2 infection of airway epithelial cultures. Am. J. Physiol. Lung Cell Mol. Physiol. 2021, 320, L750–L756. [Google Scholar] [CrossRef] [PubMed]
- Jang, Y.; Shin, H.; Lee, M.K.; Kwon, O.S.; Shin, J.S.; Kim, Y.I.; Kim, C.W.; Lee, H.R.; Kim, M. Antiviral activity of lambda-carrageenan against influenza viruses and severe acute respiratory syndrome coronavirus 2. Sci. Rep. 2021, 11, 821. [Google Scholar] [CrossRef]
- Kornberg, A.; Rao, N.N.; Ault-Riché, D. Inorganic polyphosphate: A molecule of many functions. Annu. Rev. Biochem. 1999, 68, 89–125. [Google Scholar] [CrossRef] [PubMed]
- Diaz, J.; Ingall, E.; Benitez-Nelson, C.; Paterson, D.; de Jonge, M.D.; McNulty, I.; Brandes, J.A. Marine polyphosphate: A key player in geologic phosphorus sequestration. Science 2008, 320, 652–655. [Google Scholar] [CrossRef] [PubMed]
- Ou, H.; Li, M.; Wu, S.; Jia, L.; Hill, R.T.; Zhao, J. Characteristic microbiomes correlate with polyphosphate accumulation of marine sponges in South China Sea areas. Microorganisms 2020, 8, 63. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Neufurth, M.; Wang, X.; Wang, S.; Schröder, H.C.; Müller, W.E.G. Caged dexamethasone/quercetin nanoparticles, formed of the morphogenetic active inorganic polyphosphate, are strong inducers of MUC5AC. Mar. Drugs 2021, 19, 64. [Google Scholar] [CrossRef] [PubMed]
- Müller, F.; Mutch, N.J.; Schenk, W.A.; Smith, S.A.; Esterl, L.; Spronk, H.M.; Schmidbauer, S.; Gahl, W.A.; Morrissey, J.H.; Renné, T. Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo. Cell 2009, 139, 1143–1156. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Smith, S.A.; Choi, S.H.; Davis-Harrison, R.; Huyck, J.; Boettcher, J.; Rienstra, C.M.; Morrissey, J.H. Polyphosphate exerts differential effects on blood clotting, depending on polymer size. Blood 2010, 116, 4353–4359. [Google Scholar] [CrossRef] [PubMed]
- Yang, X.; Wan, M.; Liang, T.; Peng, M.; Chen, F. Synthetic polyphosphate inhibits endogenous coagulation and platelet aggregation in vitro. Biomed. Rep. 2017, 6, 57–62. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Iba, T.; Levy, J.H.; Levi, M.; Connors, J.M.; Thachil, J. Coagulopathy of coronavirus disease 2019. Crit. Care Med. 2020, 48, 1358–1364. [Google Scholar] [CrossRef] [PubMed]
- Koupenova, M.; Freedman, J.E. Platelets and COVID-19: Inflammation, hyperactivation and additional questions. Circ. Res. 2020, 127, 1419–1421. [Google Scholar] [CrossRef] [PubMed]
- Schepler, H.; Wang, X.; Neufurth, M.; Wang, S.; Schröder, H.C.; Müller, W.E.G. The therapeutic potential of inorganic polyphosphate: A versatile physiological polymer to control coronavirus disease (COVID-19). Theranostics 2021, 11, 6193–6213. [Google Scholar] [CrossRef]
- Lempp, F.A.; Soriaga, L.B.; Montiel-Ruiz, M.; Benigni, F.; Noack, J.; Park, Y.-J.; Bianchi, S.; Walls, A.C.; Bowen, J.E.; Zhou, J.; et al. Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies. Nature 2021, 598, 342–347. [Google Scholar] [CrossRef]
- Munekata, P.E.S.; Pateiro, M.; Conte-Junior, C.A.; Domínguez, R.; Nawaz, A.; Walayat, N.; Movilla Fierro, E.; Lorenzo, J.M. Marine alkaloids: Compounds with in vivo activity and chemical synthesis. Mar. Drugs 2021, 19, 374. [Google Scholar] [CrossRef] [PubMed]
- Elissawy, A.M.; Soleiman Dehkordi, E.; Mehdinezhad, N.; Ashour, M.L.; Mohammadi Pour, P. Cytotoxic alkaloids derived from marine sponges: A comprehensive review. Biomolecules 2021, 11, 258. [Google Scholar] [CrossRef] [PubMed]
- Sachse, M.; Tenorio, R.; Fernández de Castro, I.; Muñoz-Basagoiti, J.; Perez-Zsolt, D.; Raïch-Regué, D.; Rodon, J.; Losada, A.; Avilés, P.; Cuevas, C.; et al. Unraveling the antiviral activity of plitidepsin against SARS-CoV-2 by subcellular and morphological analysis. Antivir. Res. 2022, 200, 105270. [Google Scholar] [CrossRef] [PubMed]
- Vishvakarma, V.K.; Singh, M.B.; Jain, P.; Kumari, K.; Singh, P. Hunting the main protease of SARS-CoV-2 by plitidepsin: Molecular docking and temperature-dependent molecular dynamics simulations. Amino Acids 2022, 54, 205–213. [Google Scholar] [CrossRef] [PubMed]
Protein | Amino Acids | Function |
---|---|---|
nsp1 | 180 | Leader protein |
nsp2 | 638 | Zinc-finger protein |
nsp3 | 1945 | Papain-like proteinase (PLpro) |
nsp4 | 500 | Tetra spanning transmembrane protein |
nsp5 | 306 | 3C-like proteinase (3CLpro) or main protease (Mpro) |
nsp6 | 290 | Transmembrane domain-containing protein |
nsp7 | 353 | A component of primase complex with nsp8 and nsp12 |
nsp8 | 198 | A component of primase complex with nsp7 and nsp12 |
nsp9 | 113 | ssRNA-binding protein |
nsp10 | 139 | Interacting with nsp14 and nsp16 |
nsp11 | 13 | n.d.(not defined) |
nsp12 | 932 | RNA-dependent RNA polymerase (RdRp) |
nsp13 | 601 | Helicase |
nsp14 | 527 | N7-Methyltransferase and 3′-5′ exonuclease (ExoN) |
nsp15 | 346 | Uridine-specific endoribonuclease |
nsp16 | 298 | 2′-O-ribose Methyltransferase |
Target | Marine Compound | Reference |
---|---|---|
Viral spike protein | Sulfated polysaccharides | [91] |
Inorganic polyphosphates | [92,93] | |
Phycobilins | [94] | |
Mannose-specific lectins | [95] | |
Mpro and/or PLpro | Polyphenols | [96,97] |
Alkaloids | [98,99,100,101] | |
Phycobilins | [102] | |
Coumarin derivatives | [103] | |
Naphthalene derivatives | [104] | |
RdRp | Nucleoside analogues | [105] |
TMPRSS2 | Watasenia preluciferyl β-D- glucopyranosiduronic acid | [106] |
hACE2 | Inorganic polyphosphates | [107] |
Mycosporin-like amino acids | [108] | |
Immune system | Inorganic polyphosphates | [107,109] |
Host eEF1A | Plitidepsin | [110,111] |
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Yang, Y.; Li, J.; Han, F. Focus on Marine Animal Safety and Marine Bioresources in Response to the SARS-CoV-2 Crisis. Int. J. Mol. Sci. 2022, 23, 15136. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms232315136
Yang Y, Li J, Han F. Focus on Marine Animal Safety and Marine Bioresources in Response to the SARS-CoV-2 Crisis. International Journal of Molecular Sciences. 2022; 23(23):15136. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms232315136
Chicago/Turabian StyleYang, Yao, Jiacheng Li, and Fang Han. 2022. "Focus on Marine Animal Safety and Marine Bioresources in Response to the SARS-CoV-2 Crisis" International Journal of Molecular Sciences 23, no. 23: 15136. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms232315136