4GSD

H5.3 Fab Structure

Summary for 4GSD

• Entry DOI: 10.2210/pdb4gsd/pdb
• Descriptor: H5.3 Fab Light Chain, H5.3 Fab Heavy Chain (3 entities in total)
• Functional Keywords: antibody, immune response, influenza h5 hemagglutanin, immune system
• Biological source: Homo sapiens; More
• Total number of polymer chains: 2
• Total formula weight: 46644.99

Authors

Spiller, B.W.,Winarski, K.L. (deposition date: 2012-08-27, release date: 2013-08-21, Last modification date: 2024-11-27)

Primary citation

Thornburg, N.J.,Nannemann, D.P.,Blum, D.L.,Belser, J.A.,Tumpey, T.M.,Deshpande, S.,Fritz, G.A.,Sapparapu, G.,Krause, J.C.,Lee, J.H.,Ward, A.B.,Lee, D.E.,Li, S.,Winarski, K.L.,Spiller, B.W.,Meiler, J.,Crowe, J.E.
Human antibodies that neutralize respiratory droplet transmissible H5N1 influenza viruses.
J.Clin.Invest., 123:4405-4409, 2013

PubMed Abstract: Recent studies described the experimental adaptation of influenza H5 HAs that confers respiratory droplet transmission (rdt) to influenza virus in ferrets. Acquisition of the ability to transmit via aerosol may lead to the development of a highly pathogenic pandemic H5 virus. Vaccines are predicted to play an important role in H5N1 control should the virus become readily transmissible between humans. We obtained PBMCs from patients who received an A/Vietnam/1203/2004 H5N1 subunit vaccine. Human hybridomas were then generated and characterized. We identified antibodies that bound the HA head domain and recognized both WT and rdt H5 HAs. We used a combination of structural techniques to define a mechanism of antibody recognition of an H5 HA receptor-binding site that neutralized H5N1 influenza viruses and pseudoviruses carrying the HA rdt variants that have mutations near the receptor-binding site. Incorporation or retention of this critical antigenic site should be considered in the design of novel H5 HA immunogens to protect against mammalian-adapted H5N1 mutants.

PubMed: 23999429
DOI: 10.1172/JCI69377

Experimental method

X-RAY DIFFRACTION (2.251 Å)