Comparative genome sequence analysis reveals the extent of diversity and conservation for glycan-associated proteins in burkholderia spp.

Hui San Ong, Rahmah Mohamed, Mohd Firdaus Mohd Raih

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Members of the Burkholderia family occupy diverse ecological niches. In pathogenic family members, glycan-associated proteins are often linked to functions that include virulence, protein conformation maintenance, surface recognition, cell adhesion, and immune system evasion. Comparative analysis of available Burkholderia genomes has revealed a core set of 178 glycan-associated proteins shared by all Burkholderia of which 68 are homologous to known essential genes. The genome sequence comparisons revealed insights into species-specific gene acquisitions through gene transfers, identified an S-layer protein, and proposed that significantly reactive surface proteins are associated to sugar moieties as a potential means to circumvent host defense mechanisms. The comparative analysis using a curated database of search queries enabled us to gain insights into the extent of conservation and diversity, as well as the possible virulence-associated roles of glycan-associated proteins in members of the Burkholderia spp. The curated list of glycan-associated proteins used can also be directed to screen other genomes for glycan-associated homologs.

Original languageEnglish
Article number752867
JournalComparative and Functional Genomics
Volume2012
DOIs
Publication statusPublished - 2012

Fingerprint

Burkholderia
Polysaccharides
Sequence Analysis
Genome
Proteins
Virulence
Immune Evasion
Protein Conformation
Essential Genes
Defense Mechanisms
Cell Adhesion
Genes
Immune System
Membrane Proteins
Maintenance
Databases

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Biotechnology

Cite this

@article{dd6e0e5ba3a34172ae64c5667a9b7357,
title = "Comparative genome sequence analysis reveals the extent of diversity and conservation for glycan-associated proteins in burkholderia spp.",
abstract = "Members of the Burkholderia family occupy diverse ecological niches. In pathogenic family members, glycan-associated proteins are often linked to functions that include virulence, protein conformation maintenance, surface recognition, cell adhesion, and immune system evasion. Comparative analysis of available Burkholderia genomes has revealed a core set of 178 glycan-associated proteins shared by all Burkholderia of which 68 are homologous to known essential genes. The genome sequence comparisons revealed insights into species-specific gene acquisitions through gene transfers, identified an S-layer protein, and proposed that significantly reactive surface proteins are associated to sugar moieties as a potential means to circumvent host defense mechanisms. The comparative analysis using a curated database of search queries enabled us to gain insights into the extent of conservation and diversity, as well as the possible virulence-associated roles of glycan-associated proteins in members of the Burkholderia spp. The curated list of glycan-associated proteins used can also be directed to screen other genomes for glycan-associated homologs.",
author = "Ong, {Hui San} and Rahmah Mohamed and {Mohd Raih}, {Mohd Firdaus}",
year = "2012",
doi = "10.1155/2012/752867",
language = "English",
volume = "2012",
journal = "Comparative and Functional Genomics",
issn = "1531-6912",
publisher = "Hindawi Publishing Corporation",

}

TY - JOUR

T1 - Comparative genome sequence analysis reveals the extent of diversity and conservation for glycan-associated proteins in burkholderia spp.

AU - Ong, Hui San

AU - Mohamed, Rahmah

AU - Mohd Raih, Mohd Firdaus

PY - 2012

Y1 - 2012

N2 - Members of the Burkholderia family occupy diverse ecological niches. In pathogenic family members, glycan-associated proteins are often linked to functions that include virulence, protein conformation maintenance, surface recognition, cell adhesion, and immune system evasion. Comparative analysis of available Burkholderia genomes has revealed a core set of 178 glycan-associated proteins shared by all Burkholderia of which 68 are homologous to known essential genes. The genome sequence comparisons revealed insights into species-specific gene acquisitions through gene transfers, identified an S-layer protein, and proposed that significantly reactive surface proteins are associated to sugar moieties as a potential means to circumvent host defense mechanisms. The comparative analysis using a curated database of search queries enabled us to gain insights into the extent of conservation and diversity, as well as the possible virulence-associated roles of glycan-associated proteins in members of the Burkholderia spp. The curated list of glycan-associated proteins used can also be directed to screen other genomes for glycan-associated homologs.

AB - Members of the Burkholderia family occupy diverse ecological niches. In pathogenic family members, glycan-associated proteins are often linked to functions that include virulence, protein conformation maintenance, surface recognition, cell adhesion, and immune system evasion. Comparative analysis of available Burkholderia genomes has revealed a core set of 178 glycan-associated proteins shared by all Burkholderia of which 68 are homologous to known essential genes. The genome sequence comparisons revealed insights into species-specific gene acquisitions through gene transfers, identified an S-layer protein, and proposed that significantly reactive surface proteins are associated to sugar moieties as a potential means to circumvent host defense mechanisms. The comparative analysis using a curated database of search queries enabled us to gain insights into the extent of conservation and diversity, as well as the possible virulence-associated roles of glycan-associated proteins in members of the Burkholderia spp. The curated list of glycan-associated proteins used can also be directed to screen other genomes for glycan-associated homologs.

UR - http://www.scopus.com/inward/record.url?scp=84866925603&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84866925603&partnerID=8YFLogxK

U2 - 10.1155/2012/752867

DO - 10.1155/2012/752867

M3 - Article

VL - 2012

JO - Comparative and Functional Genomics

JF - Comparative and Functional Genomics

SN - 1531-6912

M1 - 752867

ER -