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Title: The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains

Abstract

The current vaccine against smallpox is an infectious form of vaccinia virus that has significant side effects. Alternative vaccine approaches using recombinant viral proteins are being developed. A target of subunit vaccine strategies is the poxvirus protein A33, a conserved protein in the Chordopoxvirinae subfamily of Poxviridae that is expressed on the outer viral envelope. Here we have determined the structure of the A33 ectodomain of vaccinia virus. The structure revealed C-type lectin-like domains (CTLDs) that occur as dimers in A33 crystals with five different crystal lattices. Comparison of the A33 dimer models shows that the A33 monomers have a degree of flexibility in position within the dimer. Structural comparisons show that the A33 monomer is a close match to the Link module class of CTLDs but that the A33 dimer is most similar to the natural killer (NK)-cell receptor class of CTLDs. Structural data on Link modules and NK-cell receptor-ligand complexes suggest a surface of A33 that could interact with viral or host ligands. The dimer interface is well conserved in all known A33 sequences, indicating an important role for the A33 dimer. The structure indicates how previously described A33 mutations disrupt protein folding and locates the positions ofmore » N-linked glycosylations and the epitope of a protective antibody.« less

Authors:
; ; ;  [1]
  1. (NIH)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1002283
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Virol.; Journal Volume: 84; Journal Issue: (5) ; 03, 2010
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; CRYSTAL LATTICES; DIMERS; FLEXIBILITY; MONOMERS; MUTATIONS; PROTEINS; SIDE EFFECTS; TARGETS; VACCINES; VACCINIA VIRUS

Citation Formats

Su, Hua-Poo, Singh, Kavita, Gittis, Apostolos G., and Garboczi, David N. The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains. United States: N. p., 2010. Web. doi:10.1128/JVI.02247-09.
Su, Hua-Poo, Singh, Kavita, Gittis, Apostolos G., & Garboczi, David N. The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains. United States. doi:10.1128/JVI.02247-09.
Su, Hua-Poo, Singh, Kavita, Gittis, Apostolos G., and Garboczi, David N. Wed . "The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains". United States. doi:10.1128/JVI.02247-09.
@article{osti_1002283,
title = {The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains},
author = {Su, Hua-Poo and Singh, Kavita and Gittis, Apostolos G. and Garboczi, David N.},
abstractNote = {The current vaccine against smallpox is an infectious form of vaccinia virus that has significant side effects. Alternative vaccine approaches using recombinant viral proteins are being developed. A target of subunit vaccine strategies is the poxvirus protein A33, a conserved protein in the Chordopoxvirinae subfamily of Poxviridae that is expressed on the outer viral envelope. Here we have determined the structure of the A33 ectodomain of vaccinia virus. The structure revealed C-type lectin-like domains (CTLDs) that occur as dimers in A33 crystals with five different crystal lattices. Comparison of the A33 dimer models shows that the A33 monomers have a degree of flexibility in position within the dimer. Structural comparisons show that the A33 monomer is a close match to the Link module class of CTLDs but that the A33 dimer is most similar to the natural killer (NK)-cell receptor class of CTLDs. Structural data on Link modules and NK-cell receptor-ligand complexes suggest a surface of A33 that could interact with viral or host ligands. The dimer interface is well conserved in all known A33 sequences, indicating an important role for the A33 dimer. The structure indicates how previously described A33 mutations disrupt protein folding and locates the positions of N-linked glycosylations and the epitope of a protective antibody.},
doi = {10.1128/JVI.02247-09},
journal = {J. Virol.},
number = (5) ; 03, 2010,
volume = 84,
place = {United States},
year = {Wed Nov 03 00:00:00 EDT 2010},
month = {Wed Nov 03 00:00:00 EDT 2010}
}