Structure of Rotavirus Outer-Layer Protein VP7 Bound with a Neutralizing Fab-Reference-Cited by-同舟云学术

Structure of Rotavirus Outer-Layer Protein VP7 Bound with a Neutralizing Fab

Published:2009-06-12 Issue:5933 Volume:324 Page:1444-1447
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Aoki Scott T.¹,Settembre Ethan C.¹,Trask Shane D.¹,Greenberg Harry B.²,Harrison Stephen C.¹³,Dormitzer Philip R.¹

Affiliation:

1. Laboratory of Molecular Medicine, Children’s Hospital, Boston, MA 02115, USA.

2. Department of Microbiology and Immunology and Department of Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA, and VA Palo Alto Health Care System, Palo Alto, CA 94304, USA.

3. Howard Hughes Medical Institute, Children’s Hospital, Boston, MA 02115, USA.

Abstract

Rotavirus Rumbled Rotavirus infection is the primary cause of severe diarrhea in infants. For the virus to enter cells, a Ca 2+ -stabilized trimer of the outer layer protein VP7 must be dissociated. Aoki et al. (p. 1444 ) report the structure of the VP7 trimer in complex with the Fab fragment of a neutralizing monoclonal antibody. Based on the structure and an analysis of positions of neutralization escape mutations, the authors propose that many neutralizing antibodies inhibit cell entry by stabilizing the VP7 trimer even at low calcium concentrations. A disulfide-linked trimer was then produced that is a potential subunit immunogen.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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