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Start Over Author "Ki Joon Cho" Publisher american society for microbiology
2 results on '"Ki Joon Cho"'

1. Crystal Structure of the Conserved Amino Terminus of the Extracellular Domain of Matrix Protein 2 of Influenza A Virus Gripped by an Antibody

Author

Ki Joon Cho, Bert Schepens, Walter Fiers, Kristof Moonens, Xavier Saelens, Han Remaut, Lei Deng, Department of Bio-engineering Sciences, Vrije Universiteit Brussel, and Structural Biology Brussels

Subjects
0301 basic medicine, Protein Conformation, Stereochemistry, Immunology, Plasma protein binding, Antibodies, Viral, Crystallography, X-Ray, Microbiology, Epitope, Cell Line, Viral Matrix Proteins, 03 medical and health sciences, Protein structure, Virology, Animals, Humans, Neutralizing antibody, Mice, Inbred BALB C, Viral matrix protein, biology, Structure and Assembly, Antibodies, Monoclonal, Molecular biology, 030104 developmental biology, Ectodomain, Insect Science, biology.protein, Paratope, Antibody, Protein Binding
Abstract

We report the crystal structure of the M2 ectodomain (M2e) in complex with a monoclonal antibody that binds the amino terminus of M2. M2e extends into the antibody binding site to form an N-terminal β-turn near the bottom of the paratope. This M2e folding differs significantly from that of M2e in complex with an antibody that binds another part of M2e. This suggests that M2e can adopt at least two conformations that can elicit protective antibodies.

Published
2016
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2. Structure of the Extracellular Domain of Matrix Protein 2 of Influenza A Virus in Complex with a Protective Monoclonal Antibody.

Author

Ki Joon Cho, Schepens, Bert, Jong Hyeon Seok, Kim, Sella, Roose, Kenny, Ji-Hye Lee, Gallardo, Rodrigo, Van Hamme, Evelien, Schymkowiz, Joost, Rousseau, Frederic, Fiers, Walter, Saelens, Xavier, and Kyung Hyun Kim

Subjects
*INFLUENZA A virus, *VACCINE research, *IMMUNOGLOBULINS, *MONOCLONAL antibodies, *TRYPTOPHAN
Abstract

The extracellular domain of influenza A virus matrix protein 2 (M2e) is conserved and is being evaluated as a quasiuniversal influenza A vaccine candidate. We describe the crystal structure at 1.6 Å resolution of M2e in complex with the Fab fragment of an M2e-specific monoclonal antibody that protects against influenza A virus challenge. This antibody binds M2 expressed on the surfaces of cells infected with influenza A virus. Five out of six complementary determining regions interact with M2e, and three highly conserved M2e residues are critical for this interaction. In this complex, M2e adopts a compact U-shaped conformation stabilized in the center by the highly conserved tryptophan residue in M2e. This is the first description of the three-dimensional structure of M2e. [ABSTRACT FROM AUTHOR]

Published
2015
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