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Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody.

Nature communications (2015-09-16)
Tianlei Ying, Ponraj Prabakaran, Lanying Du, Wei Shi, Yang Feng, Yanping Wang, Lingshu Wang, Wei Li, Shibo Jiang, Dimiter S Dimitrov, Tongqing Zhou
ABSTRACT

The MERS-CoV is an emerging virus, which already infected more than 1,300 humans with high (∼36%) mortality. Here, we show that m336, an exceptionally potent human anti-MERS-CoV antibody, is almost germline with only one somatic mutation in the heavy chain. The structure of Fab m336 in complex with the MERS-CoV receptor-binding domain reveals that its IGHV1-69-derived heavy chain provides more than 85% binding surface and that its epitope almost completely overlaps with the receptor-binding site. Analysis of antibodies from 69 healthy humans suggests an important role of the V(D)J recombination-generated junctional and allele-specific residues for achieving high affinity of binding at such low levels of somatic hypermutation. Our results also have important implications for development of vaccine immunogens based on the newly identified m336 epitope as well as for elucidation of mechanisms of neutralization by m336-like antibodies and their elicitation in vivo.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Monoclonal ANTI-FLAG® M2-Peroxidase (HRP) antibody produced in mouse, clone M2, purified immunoglobulin, buffered aqueous glycerol solution
Sigma-Aldrich
Anti-Human IgG (Fc specific)−Peroxidase antibody produced in goat, affinity isolated antibody

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