HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Chu, S. Articles by Trust, T. J. Search for Related Content PubMed PubMed Citation Articles by Chu, S. Articles by Trust, T. J. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 266, Issue 23, 15258-15265, 08, 1991

Structure of the tetragonal surface virulence array protein and gene of Aeromonas salmonicida

S Chu, S Cavaignac, J Feutrier, BM Phipps, M Kostrzynska, WW Kay and TJ Trust
Department of Biochemistry, University of Victoria, British Columbia, Canada.

The paracrystalline surface protein array of the pathogenic bacterium Aeromonas salmonicida is a primary virulence factor with novel binding capabilities. The species-specific structural gene (vapA) for this array protein (A-protein) was cloned into lambda gt11 but was unstable when expressed in Escherichia coli, undergoing an 816-base pair deletion due to a 21-base pair direct repeat within the gene. However, the gene was stable in cosmid pLA2917 as long as expression was poor. A- protein was located in the cytoplasmic, inner membrane and periplasmic fractions in E. coli. The DNA sequence revealed a 1,506-base pair open reading frame encoding a protein consisting of a 21-amino acid signal peptide, and a 481-residue 50,778 molecular weight protein containing considerable secondary structure. When assembled into a paracrystalline protein array on Aeromonas the cell surface A-protein was totally refractile to cleavage by trypsin, but became trypsin sensitive when disassembled. Trypsin cleavage of the isolated protein provided evidence that both the NH2- and COOH-terminal regions form distinct structural domains, consistent with three-dimensional ultrastructural evidence. The NH2-terminal 274-residue domain remained refractile to trypsin activity. This segment connects by a trypsin and CNBr-sensitive 78-residue linker region to a COOH-terminal 129-residue fragment which could apparently refold into a partially trypsin-resistant structure after cleavage at residue 323.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. Najimi, M. L. Lemos, and C. R. Osorio Identification of Siderophore Biosynthesis Genes Essential for Growth of Aeromonas salmonicida under Iron Limitation Conditions Appl. Envir. Microbiol., April 15, 2008; 74(8): 2341 - 2348. [Abstract] [Full Text] [PDF]

				S. F. Gonzalez, M. J. Krug, M. E. Nielsen, Y. Santos, and D. R. Call Simultaneous Detection of Marine Fish Pathogens by Using Multiplex PCR and a DNA Microarray J. Clin. Microbiol., April 1, 2004; 42(4): 1414 - 1419. [Abstract] [Full Text] [PDF]

				S. E. Burr, K. Stuber, and J. Frey The ADP-Ribosylating Toxin, AexT, from Aeromonas salmonicida subsp. salmonicida Is Translocated via a Type III Secretion Pathway J. Bacteriol., November 15, 2003; 185(22): 6583 - 6591. [Abstract] [Full Text] [PDF]

				M. Ventura, I. Jankovic, D. C. Walker, R. D. Pridmore, and R. Zink Identification and Characterization of Novel Surface Proteins in Lactobacillus johnsonii and Lactobacillus gasseri Appl. Envir. Microbiol., December 1, 2002; 68(12): 6172 - 6181. [Abstract] [Full Text] [PDF]

				S. E. Burr, K. Stuber, T. Wahli, and J. Frey Evidence for a Type III Secretion System in Aeromonas salmonicida subsp. salmonicida J. Bacteriol., November 1, 2002; 184(21): 5966 - 5970. [Abstract] [Full Text] [PDF]

				M. Braun, K. Stuber, Y. Schlatter, T. Wahli, P. Kuhnert, and J. Frey Characterization of an ADP-Ribosyltransferase Toxin (AexT) from Aeromonas salmonicida subsp. salmonicida J. Bacteriol., April 1, 2002; 184(7): 1851 - 1858. [Abstract] [Full Text] [PDF]

				M. Sára and U. B. Sleytr S-Layer Proteins J. Bacteriol., February 15, 2000; 182(4): 859 - 868. [Full Text]

				S. Howorka, M. Sara, Y. Wang, B. Kuen, U. B. Sleytr, W. Lubitz, and H. Bayley Surface-accessible Residues in the Monomeric and Assembled Forms of a Bacterial Surface Layer Protein J. Biol. Chem., November 22, 2000; 275(48): 37876 - 37886. [Abstract] [Full Text] [PDF]