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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Khurana, Surender Dormitzer, Philip R. Liao, Hua-xin King, Lisa R. Kepler, Thomas B. Whittle, James R. R. Manischewitz, Jody Zhang, Ruijun Harrison, Stephen C. Golding, Hana Walter, Emmanuel B. Haynes, Barton F. Moody, M. Anthony |
Description | Author Affiliation: Whittle JR ( Laboratory of Molecular Medicine, Children's Hospital, Harvard Medical School and Howard Hughes Medical Institute, Boston, MA 02115, USA.); |
Abstract | Seasonal antigenic drift of circulating influenza virus leads to a requirement for frequent changes in vaccine composition, because exposure or vaccination elicits human antibodies with limited cross-neutralization of drifted strains. We describe a human monoclonal antibody, CH65, obtained by isolating rearranged heavy- and light-chain genes from sorted single plasma cells, coming from a subject immunized with the 2007 trivalent influenza vaccine. The crystal structure of a complex of the hemagglutinin (HA) from H1N1 strain A/Solomon Islands/3/2006 with the Fab of CH65 shows that the tip of the CH65 heavy-chain complementarity determining region 3 (CDR3) inserts into the receptor binding pocket on HA1, mimicking in many respects the interaction of the physiological receptor, sialic acid. CH65 neutralizes infectivity of 30 out of 36 H1N1 strains tested. The resistant strains have a single-residue insertion near the rim of the sialic-acid pocket. We conclude that broad neutralization of influenza virus can be achieved by antibodies with contacts that mimic those of the receptor. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 34 |
Volume Number | 108 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 2011-08-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | Antibodies, Neutralizing Immunology Antibody Specificity Hemagglutinin Glycoproteins, Influenza Virus Influenza A Virus, H1N1 Subtype Receptors, Virus Amino Acid Sequence Antibodies, Monoclonal Chemistry Antibodies, Viral Antibody Affinity Binding Sites Complementarity Determining Regions Glycosylation Models, Molecular Molecular Sequence Data Phylogeny Protein Binding Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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