Title |
Epitope mapping by random peptide phage display reveals essential residues for vaccinia extracellular enveloped virion spread
|
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Published in |
Virology Journal, September 2012
|
DOI | 10.1186/1743-422x-9-217 |
Pubmed ID | |
Authors |
Yong He, Yonggang Wang, Evi B Struble, Pei Zhang, Soma Chowdhury, Jennifer L Reed, Michael Kennedy, Dorothy E Scott, Robert W Fisher |
Abstract |
A33 is a type II integral membrane protein expressed on the extracellular enveloped form of vaccinia virus (VACV). Passive transfer of A33-directed monoclonal antibodies or vaccination with an A33 subunit vaccine confers protection against lethal poxvirus challenge in animal models. Homologs of A33 are highly conserved among members of the Orthopoxvirus genus and are potential candidates for inclusion in vaccines or assays targeting extracellular enveloped virus activity. One monoclonal antibody directed against VACV A33, MAb-1G10, has been shown to target a conformation-dependent epitope. Interestingly, while it recognizes VACV A33 as well as the corresponding variola homolog, it does not bind to the monkeypox homolog. In this study, we utilized a random phage display library to investigate the epitope recognized by MAb-1G10 that is critical for facilitating cell-to-cell spread of the vaccinia virus. |
X Demographics
Geographical breakdown
Country | Count | As % |
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United States | 1 | 50% |
Unknown | 1 | 50% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 50% |
Science communicators (journalists, bloggers, editors) | 1 | 50% |
Mendeley readers
Geographical breakdown
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Unknown | 42 | 100% |
Demographic breakdown
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Student > Postgraduate | 6 | 14% |
Student > Master | 5 | 12% |
Student > Bachelor | 3 | 7% |
Researcher | 3 | 7% |
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Unknown | 7 | 17% |
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Other | 5 | 12% |
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