Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractAnalysis of the clumping-mediating domain(s) of sex pheromone plasmid pAD1-encoded aggregation substance    Next AbstractNutritional Characteristics of Forage Grown in South of Benin »

Mol Microbiol


Title:"Cloning and functional analysis of Asa373, a novel adhesin unrelated to the other sex pheromone plasmid-encoded aggregation substances of Enterococcus faecalis"
Author(s):Muscholl-Silberhorn A;
Address:"Universitat Regensburg, NWFIII-Mikrobiologie, Universitatsstrasse 31, D-93053 Regensburg, Germany. albrecht.muscholl@biologie.uni-regensburg.de"
Journal Title:Mol Microbiol
Year:1999
Volume:34
Issue:3
Page Number:620 - 630
DOI: 10.1046/j.1365-2958.1999.01631.x
ISSN/ISBN:0950-382X (Print) 0950-382X (Linking)
Abstract:"pAM373 of Enterococcus faecalis deviates from the various other representatives of sex pheromone plasmids in that it encodes a clumping-mediating adhesin, Asa373, unrelated to the highly conserved aggregation substances typical of this plasmid class. The use of a new general cloning strategy and sequencing of the corresponding gene has confirmed that Asa373 represents a novel type of adhesin embedded in a DNA sequence very similar to sex pheromone plasmid pPD1. To prove the specific function of the relatively small protein (75.6 kDa vs 137 kDa for pAD1-encoded Asa1) in cell aggregation, an expression vector, pERM-ex1, was constructed, allowing reliable and stable expression of proteins in E. faecalis. The expression of Asa373 in E. faecalis indeed resulted in constitutive clumping, whereas non-polar disruption of the gene in the original pAM373 abolished clumping capacity. Expression in a strain (INY3000) defective in binding substance - which for the other aggregation substances constitutes the attachment site on the mating partner - did not alter Asa373-dependent clumping; this implies a separate mechanism in cell-cell interaction for this adhesin. Some amino acid motifs of Asa373 link the protein to adhesins of oral streptococci and other cell surface proteins. Comparison of the leader sequence of asa373 with those of several other aggregation substances revealed a highly conserved translational unit possibly involved in the regulation of asa373 expression"
Keywords:"Adhesins, Bacterial/chemistry/genetics/*metabolism Amino Acid Sequence Bacterial Proteins/genetics Base Sequence Cell Aggregation/genetics *Cloning, Molecular Enterococcus faecalis/*genetics/metabolism Molecular Sequence Data Pheromones/genetics Plasmids/;"
Notes:"MedlineMuscholl-Silberhorn, A eng Research Support, Non-U.S. Gov't England 1999/11/17 Mol Microbiol. 1999 Nov; 34(3):620-30. doi: 10.1046/j.1365-2958.1999.01631.x"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-09-2024