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

2015 ◽  
Vol 90 (1) ◽  
pp. 611-615 ◽  
Author(s):  
Ki Joon Cho ◽  
Bert Schepens ◽  
Kristof Moonens ◽  
Lei Deng ◽  
Walter Fiers ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Monoclonal Antibody ◽  
Binding Site ◽  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Antibody Binding ◽  
Amino Terminus ◽  
Antibody Binding Site ◽  
Protective Antibodies

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.

Location and architecture of an antibody-binding site of influenza A virus nucleoprotein

2013 ◽  
Vol 159 (6) ◽  
pp. 1493-1497 ◽  
Author(s):  
Natalia L. Varich ◽  
Galina K. Sadykova ◽  
Alexei G. Prilipov ◽  
Konstantin S. Kochergin-Nikitsky ◽  
Robert G. Webster ◽  
...  
Keyword(s):  
Binding Site ◽  
Influenza A Virus ◽  
Influenza A ◽  
Antibody Binding ◽  
Antibody Binding Site

scholarly journals Crystal structure of an orthomyxovirus matrix protein reveals mechanisms for self-polymerization and membrane association

2017 ◽  
Vol 114 (32) ◽  
pp. 8550-8555 ◽  
Author(s):  
Wenting Zhang ◽  
Wenjie Zheng ◽  
Yukimatsu Toh ◽  
Miguel A. Betancourt-Solis ◽  
Jiagang Tu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Crystal Lattice ◽  
Influenza A Virus ◽  
Nuclear Export ◽  
Influenza A ◽  
Electrostatic Interactions ◽  
Matrix Protein ◽  
Structural Integrity ◽  
Viral Envelope ◽  
Protein Layer

Many enveloped viruses encode a matrix protein. In the influenza A virus, the matrix protein M1 polymerizes into a rigid protein layer underneath the viral envelope to help enforce the shape and structural integrity of intact viruses. The influenza virus M1 is also known to mediate virus budding as well as the nuclear export of the viral nucleocapsids and their subsequent packaging into nascent viral particles. Despite extensive studies on the influenza A virus M1 (FLUA-M1), only crystal structures of its N-terminal domain are available. Here we report the crystal structure of the full-length M1 from another orthomyxovirus that infects fish, the infectious salmon anemia virus (ISAV). The structure of ISAV-M1 assumes the shape of an elbow, with its N domain closely resembling that of the FLUA-M1. The C domain, which is connected to the N domain through a flexible linker, is made of four α-helices packed as a tight bundle. In the crystal, ISAV-M1 monomers form infinite 2D arrays with a network of interactions involving both the N and C domains. Results from liposome flotation assays indicated that ISAV-M1 binds membrane via electrostatic interactions that are primarily mediated by a positively charged surface loop from the N domain. Cryoelectron tomography reconstruction of intact ISA virions identified a matrix protein layer adjacent to the inner leaflet of the viral membrane. The physical dimensions of the virion-associated matrix layer are consistent with the 2D ISAV-M1 crystal lattice, suggesting that the crystal lattice is a valid model for studying M1–M1, M1–membrane, and M1–RNP interactions in the virion.

Characterization of a fully human monoclonal antibody against extracellular domain of matrix protein 2 of influenza A virus

2011 ◽  
Vol 91 (3) ◽  
pp. 283-287 ◽  
Author(s):  
Tatsuhiko Ozawa ◽  
Aishun Jin ◽  
Kazuto Tajiri ◽  
Masaya Takemoto ◽  
Tomoko Okuda ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Human Monoclonal Antibody ◽  
Extracellular Domain

Pentapeptide Identified as a Monoclonal Antibody Binding Site in the Serine-Protease Domain of t-PA

1994 ◽  
Vol 375 (7) ◽  
pp. 471-480 ◽  
Author(s):  
Frank O. Gombert ◽  
William Werz ◽  
Michael Schlüter ◽  
Anja Bayer ◽  
Rolf G. Werner ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Binding Site ◽  
Serine Protease ◽  
Antibody Binding ◽  
Protease Domain ◽  
Serine Protease Domain ◽  
Antibody Binding Site ◽  
Monoclonal Antibody Binding

Monoclonal antibody binding-site diversity assessment with a cell-based clustering assay

2014 ◽  
Vol 405 ◽  
pp. 1-14 ◽  
Author(s):  
Sindy Liao-Chan ◽  
Joseph Zachwieja ◽  
Steven Gomez ◽  
Dana Duey ◽  
John Lippincott ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Binding Site ◽  
Antibody Binding ◽  
Antibody Binding Site ◽  
Diversity Assessment ◽  
A Cell ◽  
Site Diversity ◽  
Monoclonal Antibody Binding

scholarly journals A GFP Expressing Influenza A Virus to Report In Vivo Tropism and Protection by a Matrix Protein 2 Ectodomain-Specific Monoclonal Antibody

PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0121491 ◽  
Author(s):  
Sarah De Baets ◽  
Judith Verhelst ◽  
Silvie Van den Hoecke ◽  
Anouk Smet ◽  
Michael Schotsaert ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Specific Monoclonal Antibody

Human single chain monoclonal antibody that recognizes matrix protein of heterologous influenza A virus subtypes

2009 ◽  
Vol 159 (1) ◽  
pp. 105-111 ◽  
Author(s):  
Ornnuthchar Poungpair ◽  
Wanpen Chaicumpa ◽  
Kasem Kulkeaw ◽  
Santi Maneewatch ◽  
Kanyarat Thueng-in ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Single Chain

Oligosaccharide recognition by antibodies: Synthesis and evaluation of talose oligosaccharide analogues

2002 ◽  
Vol 80 (8) ◽  
pp. 1112-1130 ◽  
Author(s):  
T L Lowary ◽  
E Eichler ◽  
D R Bundle
Keyword(s):  
Monoclonal Antibody ◽  
Molecular Recognition ◽  
Binding Site ◽  
Antibody Binding ◽  
Solution Phase ◽  
O Antigen ◽  
Antibody Binding Site ◽  
Alkyl Groups ◽  
Galactose Residue ◽  
Native Ligand

A series of monosaccharide (4–6), disaccharide (3,7–12), and trisaccharide (13–15) analogs of the native ligand 2, which fills the binding site of monoclonal antibody Se 155.4, have been synthesized and their bioactivity measured by solid- and solution-phase assays. The syntheses of disaccharide analogs sought to replace galactose by various alkyl groups at the O-2 position of mannose. The activity of one of these O-2 alkyl analogs was 75% of that observed for the trisaccharide and points to only weak net bonding between the solvent exposed galactose residue and the antibody binding site. The synthesis of talose analogs 13 and 14, where the mannose or galactose residues of 2 were replaced by talose produced ligands with activities from one-third to one-half of that seen for the native ligand 2. These activity changes did not exhibit discernable correlations with the ability of talose to disrupt water of solvation.Key words: abequose, 3,6-dideoxy-D-xylo-hexose, talose disaccharide and trisaccharide, antibody oligosaccharide interactions, molecular recognition of carbohydrates, water in antibody complexes, Salmonella LPS, monoclonal antibody Se 155.4, bacterial O-antigen.

scholarly journals Structure of the Extracellular Domain of Matrix Protein 2 of Influenza A Virus in Complex with a Protective Monoclonal Antibody

2015 ◽  
Vol 89 (7) ◽  
pp. 3700-3711 ◽  
Author(s):  
Ki Joon Cho ◽  
Bert Schepens ◽  
Jong Hyeon Seok ◽  
Sella Kim ◽  
Kenny Roose ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Three Dimensional ◽  
Extracellular Domain ◽  
Dimensional Structure ◽  
Specific Monoclonal Antibody ◽  
Fab Fragment ◽  
Three Dimensional Structure

ABSTRACTThe 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.IMPORTANCEM2e of influenza A is under investigation as a universal influenza A vaccine, but its three-dimensional structure is unknown. We describe the structure of M2e stabilized with an M2e-specific monoclonal antibody that recognizes natural M2. We found that the conserved tryptophan is positioned in the center of the U-shaped structure of M2e and stabilizes its conformation. The structure also explains why previously reportedin vivoescape viruses, selected with a similar monoclonal antibody, carried proline residue substitutions at position 10 in M2.

Sign in / Sign up

Export Citation Format

Share Document