5DUR

Influenza A virus H5 hemagglutinin globular head in complex with antibody 100F4

Summary for 5DUR

• Entry DOI: 10.2210/pdb5dur/pdb
• Related: 5DUM 5DUP 5DUT
• Descriptor: Heavy Chain of Antibody 100F4, Light Chain of Antibody 100F4, Hemagglutinin, ... (5 entities in total)
• Functional Keywords: influenza virus, antibody, complex, neutralize, immune system
• Biological source: Homo sapiens; More
• Total number of polymer chains: 6
• Total formula weight: 148189.20

Authors

Zuo, T.,Sun, J.,Wang, G.,Zhou, P.,Wang, X.,Zhang, L. (deposition date: 2015-09-20, release date: 2015-12-16, Last modification date: 2024-10-09)

Primary citation

Zuo, T.,Sun, J.,Wang, G.,Jiang, L.,Zuo, Y.,Li, D.,Shi, X.,Liu, X.,Fan, S.,Ren, H.,Hu, H.,Sun, L.,Zhou, B.,Liang, M.,Zhou, P.,Wang, X.,Zhang, L.
Comprehensive analysis of antibody recognition in convalescent humans from highly pathogenic avian influenza H5N1 infection
Nat Commun, 6:8855-8855, 2015

PubMed Abstract: Understanding the mechanism of protective antibody recognition against highly pathogenic avian influenza A virus H5N1 in humans is critical for the development of effective therapies and vaccines. Here we report the crystal structure of three H5-specific human monoclonal antibodies bound to the globular head of hemagglutinin (HA) with distinct epitope specificities, neutralization potencies and breadth. A structural and functional analysis of these epitopes combined with those reported elsewhere identifies four major vulnerable sites on the globular head of H5N1 HA. Chimeric and vulnerable site-specific mutant pseudoviruses are generated to delineate broad neutralization specificities of convalescent sera from two individuals who recovered from the infection with H5N1 virus. Our results show that the four vulnerable sites on the globular head rather than the stem region are the major neutralizing targets, suggesting that during natural H5N1 infection neutralizing antibodies against the globular head work in concert to provide protective antibody-mediated immunity.

PubMed: 26635249
DOI: 10.1038/ncomms9855

Experimental method

X-RAY DIFFRACTION (2.82 Å)