Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment specific for an influenza virus haemagglutinin and of an escape mutant of that haemagglutinin.
Preliminary crystallographic data are given for two molecules involved in the interaction between the humoral immune response and the influenza virus. These molecules are the Fab fragment of an antibody specific for the haemagglutinin of influenza virus strain X31 (Hong Kong 1/68 (H3N2)) and a mutant of X31 haemagglutinin that escapes recognition by that antibody. Crystals of the haemagglutinin are isomorphous to those of X31, whose structure is known; they diffract to 3.4 A resolution. Crystals of the Fab fragment are trigonal with space group P3(1)21 (or P3(2)21) and diffract to 2.6 A resolution. The unit cell dimensions are a = b = 98.9 A, c = 89.2 A. A native data set has been collected for both proteins.
Bizebard
T
T
Laboratoire de Biologie Physicochimique, C.N.R.S., URA 1131 Université Paris Sud, Orsay, France.
Mauguen
Y
Y
Petek
F
F
Rigolet
P
P
Skehel
J J
JJ
Knossow
M
M
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry; D000940:Antigenic Variation / Q000276:immunology; D003460:Crystallization; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000235:genetics / Q000276:immunology*; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry; D051379:Mice; D009154:Mutation; D014961:X-Ray Diffraction
D000911:Antibodies, Monoclonal; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D007140:Immunoglobulin Fab Fragments