Fully Human Monoclonal Antibody Directed to Proteolytic Cleavage Site in Severe Acute Respiratory Syndrome (SARS) Coronavirus S Protein Neutralizes the Virus in a Rhesus Macaque SARS Model

Miyoshi‐Akiyama, Tohru; Fukushi, Masaya; Yamaguchi, Keina; Matsuoka, Yusuke; Ishihara, Takashi; Tsukahara, Masayoshi; Hatakeyama, Seisuke; Itoh, Norikazu; Morisawa, Aki; Yoshinaka, Yoshiyuki; Yamamoto, Naoki; Zhang, Lianfeng; Qin, Chuan; Kirikae, Teruo; Sasazuki, Takehiko

doi:10.1093/infdis/jir084

Cited by 38 publications

(39 citation statements)

References 31 publications

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“…We further demonstrated that the neutralizing activity induced by the SP3 peptide was specific for the postbinding and membrane fusion steps of MERS infection. Our data are consistent with a previous report on SARS-CoV (17), which indicated that human monoclonal antibody (5H10) directed to proteolytic cleavage site (791-805 amino acid) in S neutralized the virus in a rhesus macaque SARS model. Since multiple neutralizing epitopes have been identified on the S protein of SARS-CoV and envelope of HIV-1 (3,10,13,17), it is not unusual to find more than one neutralizing epitope on the MERS-CoV S protein.…”

Section: Discussionsupporting

confidence: 93%

The Amino Acids 736–761 of the MERS-CoV Spike Protein Induce Neutralizing Antibodies: Implications for the Development of Vaccines and Antiviral Agents

et al. 2014

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Based on a bioinformatics analysis of the Middle East respiratory syndrome coronavvirus (MERS-CoV) S protein, we synthesized a panel of peptides coupled to keyhole limpet haemocyanin and used them to raise antibodies in rabbits. In addition, the recombinant receptor-binding domain (RBD) was used to raise polyclonal antibodies in mice. All of the antibodies raised by S-peptide immunisation were specific and sensitive for S protein expressed in transfected cells in the indirect immunofluorescence assay or Western blotting. The RBD efficiently elicited neutralizing antibodies against MERS-CoV by blocking viral entry at the binding step. Furthermore, we found that the SP3 peptide, corresponding to amino-acid residues 736-761 of the S protein, elicited robust neutralizing activities by blocking viral entry at the postbinding and membrane fusion steps. We conclude that amino-acid residues 736-761 of the S protein carry neutralizing epitopes that may be used in the development of vaccines and antiviral agents against MERS-CoV.

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Section: Discussionsupporting

confidence: 93%

The Amino Acids 736–761 of the MERS-CoV Spike Protein Induce Neutralizing Antibodies: Implications for the Development of Vaccines and Antiviral Agents

et al. 2014

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“…Antibodies against RBD and S2 domain of SARS-CoV and MERS-CoV S proteins have been found effective in neutralizing infections of permissive cell lines in vitro [52][53][54][55]. In addition, neutralizing antibodies were capable of treating infections in experimental animals and in infected patients during these major outbreaks [56][57][58][59]. In one study, several SARS-CoV RBD-specific monoclonal antibodies did not bind to SARS-CoV-2 S protein [43].…”

Section: Of 15mentioning

confidence: 99%

Insights into the Recent 2019 Novel Coronavirus (SARS-CoV-2) in Light of Past Human Coronavirus Outbreaks

et al. 2020

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Coronaviruses (CoVs) are RNA viruses that have become a major public health concern since the Severe Acute Respiratory Syndrome-CoV (SARS-CoV) outbreak in 2002. The continuous evolution of coronaviruses was further highlighted with the emergence of the Middle East Respiratory Syndrome-CoV (MERS-CoV) outbreak in 2012. Currently, the world is concerned about the 2019 novel CoV (SARS-CoV-2) that was initially identified in the city of Wuhan, China in December 2019. Patients presented with severe viral pneumonia and respiratory illness. The number of cases has been mounting since then. As of late February 2020, tens of thousands of cases and several thousand deaths have been reported in China alone, in addition to thousands of cases in other countries. Although the fatality rate of SARS-CoV-2 is currently lower than SARS-CoV, the virus seems to be highly contagious based on the number of infected cases to date. In this review, we discuss structure, genome organization, entry of CoVs into target cells, and provide insights into past and present outbreaks. The future of human CoV outbreaks will not only depend on how the viruses will evolve, but will also depend on how we develop efficient prevention and treatment strategies to deal with this continuous threat.

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“…ACE2 as a receptor for viral entry [3,10], several SARS-CoV RBD-directed mAbs did 2 0 6 not cross-react with SARS-CoV-2 RBD [27,28]. To CoV [29][30][31]. To CoV [29][30][31].…”

Section: Mab1a9 Binds To S Expressed In Sars-cov-2-infected Cellsmentioning

confidence: 99%

Monoclonal antibodies for the S2 subunit of spike of SARS-CoV cross-react with the newly-emerged SARS-CoV-2

Zheng

Monteil

Maurer‐Stroh

et al. 2020

Preprint

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Fully Human Monoclonal Antibody Directed to Proteolytic Cleavage Site in Severe Acute Respiratory Syndrome (SARS) Coronavirus S Protein Neutralizes the Virus in a Rhesus Macaque SARS Model

Abstract: This study represents a platform to produce fully human antibodies against emerging infectious diseases in a timely and safe manner.

Cited by 38 publications

References 31 publications

The Amino Acids 736–761 of the MERS-CoV Spike Protein Induce Neutralizing Antibodies: Implications for the Development of Vaccines and Antiviral Agents

The Amino Acids 736–761 of the MERS-CoV Spike Protein Induce Neutralizing Antibodies: Implications for the Development of Vaccines and Antiviral Agents

Insights into the Recent 2019 Novel Coronavirus (SARS-CoV-2) in Light of Past Human Coronavirus Outbreaks

Monoclonal antibodies for the S2 subunit of spike of SARS-CoV cross-react with the newly-emerged SARS-CoV-2

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