How antibodies recognize virus proteins

P M Colman; G M Air; R G Webster; J N Varghese; A T Baker; M R Lentz; P A Tulloch; W G Laver

doi:10.1016/0167-5699(87)90004-1

How antibodies recognize virus proteins

Immunol Today. 1987;8(11):323-6. doi: 10.1016/0167-5699(87)90004-1.

Authors

P M Colman¹, G M Air², R G Webster³, J N Varghese¹, A T Baker¹, M R Lentz², P A Tulloch¹, W G Laver⁴

Affiliations

¹ CSIRO, Division of Protein Chemistry, 343 Royal Parade, Parkville, Victoria 3052, Australia.
² Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
³ St Jude Children's Research Hospital, PO Box 318, Memphis, TN 38101, USA.
⁴ Influenza Research Unit, JCSMR, GPO Box 334, Canberra ACT 2601, Australia.

PMID: 25291054
DOI: 10.1016/0167-5699(87)90004-1

Abstract

Numerous studies have addressed the nature of antibody-antigen interaction, but only recently have three-dimensional structures of complexes of antibodies with protein antigens been reported, one with lysozyme and one with the influenza virus antigen neuraminidase. Both structures show that there are epitopes involving about 16 amino acids on surface loops of the antigen. In the lysozyme complex the interaction of the components is rigid, but there is a degree of structural flexibility in the formation of the complex with neuraminidase. In this article, Peter Colman, Graeme Laver and their colleagues discuss some speculative implications of the results currently available.