Structure of the Neisserial Outer Membrane Protein Opa60: Loop Flexibility Essential to Receptor Recognition and Bacterial Engulfment-Reference-Cited by-同舟云学术

Structure of the Neisserial Outer Membrane Protein Opa60: Loop Flexibility Essential to Receptor Recognition and Bacterial Engulfment

Published:2014-05-19 Issue:28 Volume:136 Page:9938-9946
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Fox Daniel A.¹,Larsson Per²,Lo Ryan H.¹,Kroncke Brett M.¹,Kasson Peter M.²,Columbus Linda¹²

Affiliation:

1. Department of Chemistry, University of Virginia, Charlottesville, Virginia 22904, United States

2. Center for Membrane Biology and Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908, United States

Funder

National Science Foundation

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja503093y

Reference49 articles.

1. Relative Contributions of Recombination and Mutation to the Diversification of the opa Gene Repertoire of Neisseria gonorrhoeae

2. Carcinoembryonic Antigen Family Receptor Recognition by Gonococcal Opa Proteins Requires Distinct Combinations of Hypervariable Opa Protein Domains

3. Proteoglycan receptor binding by Neisseria gonorrhoeae MS11 is determined by the HV-1 region of OpaA

4. Critical determinants of host receptor targeting by Neisseria meningitidis and Neisseria gonorrhoeae : identification of Opa adhesiotopes on the N-domain of CD66 molecules

5. Opa proteins and CEACAMs: pathways of immune engagement for pathogenicNeisseria

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