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Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric

Ashish1, Ashish K Solanki, Christopher D Boone

  • 1Institute of Microbial Technology, Sector 39-A, Chandigarh 160036, India. ashgang@imtech.res.in

Biochemical and Biophysical Research Communications
|December 10, 2009
PubMed

Human antibody IgG1 b12 is one of the four antibodies known to neutralize a broad range of human immunodeficiency virus-1. The crystal structure of this antibody displayed an asymmetric disposition of the Fab arms relative to its Fc portion. Comparison of structures solved for other IgG1 antibodies led to a notion that crystal packing forces entrapped a "snap-shot" of different conformations accessible to this antibody. To elucidate global structure of this unique antibody, we acquired small-angle X-ray scattering data from its dilute solution. Data analysis indicated that b12 adopts a bilobal globular structure in solution with a radius of gyration and a maximum linear dimension of approximately 54 and approximately 180A, respectively. Extreme similarity between its solution and crystal structure concludes that non-flexible, asymmetric shape is an inherent property of this rare antibody.

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