Stealth proteins: in silico identification of a novel protein family rendering bacterial pathogens invisible to host immune defense.
Details
State: Public
Version: author
Serval ID
serval:BIB_37943
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Stealth proteins: in silico identification of a novel protein family rendering bacterial pathogens invisible to host immune defense.
Journal
PLoS Computational Biology
ISSN
1553-7358
Publication state
Published
Issued date
2005
Volume
1
Number
6
Pages
e63
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't --- Old uritopublisher value: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16299590
Abstract
There are a variety of bacterial defense strategies to survive in a hostile environment. Generation of extracellular polysaccharides has proved to be a simple but effective strategy against the host's innate immune system. A comparative genomics approach led us to identify a new protein family termed Stealth, most likely involved in the synthesis of extracellular polysaccharides. This protein family is characterized by a series of domains conserved across phylogeny from bacteria to eukaryotes. In bacteria, Stealth (previously characterized as SacB, XcbA, or WefC) is encoded by subsets of strains mainly colonizing multicellular organisms, with evidence for a protective effect against the host innate immune defense. More specifically, integrating all the available information about Stealth proteins in bacteria, we propose that Stealth is a D-hexose-1-phosphoryl transferase involved in the synthesis of polysaccharides. In the animal kingdom, Stealth is strongly conserved across evolution from social amoebas to simple and complex multicellular organisms, such as Dictyostelium discoideum, hydra, and human. Based on the occurrence of Stealth in most Eukaryotes and a subset of Prokaryotes together with its potential role in extracellular polysaccharide synthesis, we propose that metazoan Stealth functions to regulate the innate immune system. Moreover, there is good reason to speculate that the acquisition and spread of Stealth could be responsible for future epidemic outbreaks of infectious diseases caused by a large variety of eubacterial pathogens. Our in silico identification of a homologous protein in the human host will help to elucidate the causes of Stealth-dependent virulence. At a more basic level, the characterization of the molecular and cellular function of Stealth proteins may shed light on fundamental mechanisms of innate immune defense against microbial invasion.
Keywords
Amino Acid Sequence, Animals, Bacteria, Bacterial Infections, Computational Biology, Conserved Sequence, Evolution, Molecular, Genome, Humans, Molecular Sequence Data, Phylogeny, Proteins, Sequence Alignment, Streptomyces coelicolor, Virulence Factors
OAI-PMH
Pubmed
Web of science
Open Access
Yes
Create date
19/11/2007 13:36
Last modification date
20/08/2019 14:26