scholarly journals Full-length three-dimensional structure of the influenza A virus M1 protein and its organization into a matrix layer

PLoS Biology ◽  
2020 ◽  
Vol 18 (9) ◽  
pp. e3000827
Author(s):  
Lisa Selzer ◽  
Zhaoming Su ◽  
Grigore D. Pintilie ◽  
Wah Chiu ◽  
Karla Kirkegaard
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Three Dimensional ◽  
Full Length ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
M1 Protein ◽  
Matrix Layer

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.

scholarly journals Three-Dimensional Structure of Full Length Integrin Embedded in Membrane

2011 ◽  
Vol 17 (S2) ◽  
pp. 90-91 ◽  
Author(s):  
X-P Xu ◽  
E Kim ◽  
S Harvey ◽  
M Swift ◽  
J Smith ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Full Length ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Extended abstract of a paper presented at Microscopy and Microanalysis 2011 in Nashville, Tennessee, USA, August 7–August 11, 2011.

scholarly journals Three dimensional structure of full-length plasminogen

2012 ◽  
Vol 23 (5) ◽  
pp. 516-519
Author(s):  
Masashi AKIYAMA ◽  
Hidenori HIRAI ◽  
Toshiyuki MIYATA
Keyword(s):  
Three Dimensional ◽  
Full Length ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Three-dimensional Structure of Influenza A N9 Neuraminidase and Its Complex with the Inhibitor 2-Deoxy 2,3-Dehydro-N-Acetyl Neuraminic Acid

1993 ◽  
Vol 232 (4) ◽  
pp. 1069-1083 ◽  
Author(s):  
P. Bossart-Whitaker ◽  
M. Carson ◽  
Y.S. Babu ◽  
C.D. Smith ◽  
W.G. Laver ◽  
...  
Keyword(s):  
Influenza A ◽  
Three Dimensional ◽  
Neuraminic Acid ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Full-length cDNA cloning and protein three-dimensional structure modeling of porcine prothrombin

2007 ◽  
Vol 38 (2) ◽  
pp. 93-99 ◽  
Author(s):  
Younan Chen ◽  
Weidong Tan ◽  
Xiaofeng Lu ◽  
Yanrong Lu ◽  
Shengfang Qin ◽  
...  
Keyword(s):  
Cdna Cloning ◽  
Three Dimensional ◽  
Full Length ◽  
Dimensional Structure ◽  
Structure Modeling ◽  
Three Dimensional Structure ◽  
Full Length Cdna

scholarly journals Three-Dimensional Structure of Full Length Integrin Embedded in Membrane

2012 ◽  
Vol 102 (3) ◽  
pp. 231a-232a
Author(s):  
Xiao-Ping Xu ◽  
Eldar Kim ◽  
Sheryl Harvey ◽  
Mark Swift ◽  
Jeffrey W. Smith ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Full Length ◽  
Dimensional Structure ◽  
Three Dimensional Structure

scholarly journals Structural Differences among Hemagglutinins of Influenza A Virus Subtypes Are Reflected in Their Antigenic Architecture: Analysis of H9 Escape Mutants

2004 ◽  
Vol 78 (1) ◽  
pp. 240-249 ◽  
Author(s):  
Nikolai V. Kaverin ◽  
Irina A. Rudneva ◽  
Natalia A. Ilyushina ◽  
Aleksandr S. Lipatov ◽  
Scott Krauss ◽  
...  
Keyword(s):  
Hong Kong ◽  
Amino Acid ◽  
Influenza A ◽  
Three Dimensional ◽  
Antigenic Site ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Equivalent Site ◽  
Escape Mutants ◽  
Phenotypic Variations

ABSTRACT We used a panel of monoclonal antibodies to H9 hemagglutinin to select 18 escape mutants of mouse-adapted influenza A/Swine/Hong Kong/9/98 (H9N2) virus. Cross-reactions of the mutants with the antibodies and the sequencing of hemagglutinin genes revealed two minimally overlapping epitopes. We mapped the amino acid changes to two areas of the recently reported three-dimensional structure of A/Swine/Hong Kong/9/98 hemagglutinin. The grouping of the antigenically relevant amino acid positions in H9 hemagglutinin differs from the pattern observed in H3 and H5 hemagglutinins. Several positions in site B of H3 hemagglutinin are distributed in two sites of H9 hemagglutinin. Unlike any subtype analyzed so far, H9 hemagglutinin does not contain an antigenic site corresponding to site A in H3 hemagglutinin. Positions 145 and 193 (H3 numbering), which in H3 hemagglutinin belong to sites A and B, respectively, are within one site in H9 hemagglutinin. This finding is consistent with the peculiarity of the three-dimensional structure of the H9 molecule, that is, the absence from H9 hemagglutinin of the lateral loop that forms site A in H3 and the equivalent site in H5 hemagglutinins. The escape mutants analyzed displayed phenotypic variations, including decreased virulence for mice and changes in affinity for sialyl substrates. Our results demonstrate a correlation between intersubtype differences in three-dimensional structure and variations among subtypes in the distribution of antigenic areas. Our findings also suggest that covariation and pleiotropic effects of antibody-selected mutations may be important in the evolution of H9 influenza virus, a possible causative agent of a future pandemic.

scholarly journals Structural Determinants of the Interactions Between Influenza A Virus Matrix Protein M1 and Lipid Membranes

2018 ◽  
Author(s):  
C.T. Höfer ◽  
S. Di Lella ◽  
I. Dahmani ◽  
N. Jungnick ◽  
N. Bordag ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Structural Changes ◽  
Full Length ◽  
Image Correlation ◽  
Host Cell Membrane ◽  
M1 Protein ◽  
Animal Populations ◽  
Matrix Protein M1

ABSTRACTInfluenza A virus is a pathogen responsible for severe seasonal epidemics threatening human and animal populations every year. One of the ten proteins encoded by the viral genome, the matrix protein M1, is abundantly produced in infected cells and plays a structural role in determining the morphology of the virus. During assembly of new viral particles, M1 is recruited to the host cell membrane where it associates with lipids and other viral proteins. The structure of M1 is only partially known. In particular, structural details of M1 interactions with the cellular plasma membrane as well as M1–protein interactions and multimerization have not been clarified, yet.In this work, we employed a set of complementary experimental and theoretical tools to tackle these issues. Using raster image correlation, surface plasmon resonance and circular dichroism spectroscopies, we quantified membrane association and oligomerization of full-length M1 and of different genetically engineered M1 constructs (i.e., N- and C-terminally truncated constructs and a mutant of the polybasic region, residues 95-105). Furthermore, we report novel information on structural changes in M1 occurring upon binding to membranes. Our experimental results are corroborated by an all-atom model of the full-length M1 protein bound to a negatively charged lipid bilayer.

Three-Dimensional Structure of Full-Length NtrX, an Unusual Member of the NtrC Family of Response Regulators

2017 ◽  
Vol 429 (8) ◽  
pp. 1192-1212 ◽  
Author(s):  
Ignacio Fernández ◽  
Irina Cornaciu ◽  
Mariela del Carmen Carrica ◽  
Emiko Uchikawa ◽  
Guillaume Hoffmann ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Full Length ◽  
Dimensional Structure ◽  
Response Regulators ◽  
Three Dimensional Structure
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