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      Streptococcus pneumoniae IgA1 protease: A metalloprotease that can catalyze in a split manner in vitro

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          Abstract

          IgA1 proteases (IgA1P) from diverse pathogenic bacteria specifically cleave human immunoglobulin A1 (IgA1) at the hinge region, thereby thwarting protective host immune responses. Streptococcus pneumoniae ( S. pneumoniae) IgA1P shares no sequence conservation with serine or cysteine types of IgA1Ps or other known proteins, other than a conserved HExxH Zn‐binding motif (1604‐1608) found in metalloproteases. We have developed a novel expression system to produce the mature S. pneumoniae IgA1P and we have discovered that this form is both attached to the bacterial cell surface and released in its full form. Our data demonstrate that the S. pneumoniae IgA1P comprises two distinct regions that associate to form an active metalloprotease, the first such example of a metalloprotease that can be split in vitro and recombined to form an active enzyme. By capitalizing on this novel domain architecture, we show that the N‐terminal region of S. pneumoniae IgA1P comprises the primary binding region for IgA1, although the C‐terminal region of S. pneumoniae IgA1P is necessary for cleavage of IgA1. Our findings lend insight into the protein domain architecture of the S. pneumoniae IgA1P and function of this important virulence factor for S. pneumoniae infection.

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          Author and article information

          Contributors
          Elan.Eisenmesser@ucdenver.edu
          Journal
          Protein Sci
          Protein Sci
          10.1002/(ISSN)1469-896X
          PRO
          Protein Science : A Publication of the Protein Society
          John Wiley and Sons Inc. (Hoboken )
          0961-8368
          1469-896X
          23 February 2017
          March 2017
          : 26
          : 3 ( doiID: 10.1002/pro.v26.3 )
          : 600-610
          Affiliations
          [ 1 ] Departments of Biochemistry and Molecular Genetics University of Colorado Denver Aurora CO
          [ 2 ] Mucosal and Vaccine Research Program Colorado (MAVRC), University of Colorado Denver Aurora CO
          [ 3 ] Denver Veterans Affairs Medical Center Denver CO
          Author notes
          [*] [* ]Correspondence to: Elan Eisenmesser, 12801 East 17th Ave, Aurora, CO 80045. E‐mail: Elan.Eisenmesser@ 123456ucdenver.edu
          Article
          PMC5326571 PMC5326571 5326571 PRO3110
          10.1002/pro.3110
          5326571
          28028839
          2187c692-8dea-4ebe-976f-be081a13c069
          © 2016 The Protein Society
          History
          : 11 July 2016
          : 01 December 2016
          : 21 December 2016
          Page count
          Figures: 4, Tables: 0, Pages: 11, Words: 6364
          Funding
          Funded by: NIH
          Award ID: AI092468
          Award ID: RO1GM107262
          Award ID: 108479
          Funded by: University of Colorado Denver Mucosal and Vaccine Research Program Colorado (MAVRC) and Veterans Affairs Research Service
          Categories
          Article
          Articles
          Custom metadata
          2.0
          pro3110
          March 2017
          Converter:WILEY_ML3GV2_TO_NLMPMC version:5.0.7 mode:remove_FC converted:25.02.2017

          IgA1 protease,streptococcal pneumoniae,metalloprotease,protease turnover,split protease

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