2015
DOI: 10.1128/mbio.01339-15
|View full text |Cite
|
Sign up to set email alerts
|

A Phase-Variable Surface Layer from the Gut Symbiont Bacteroides thetaiotaomicron

Abstract: The capsule from Bacteroides, a common gut symbiont, has long been a model system for studying the molecular mechanisms of host-symbiont interactions. The Bacteroides capsule is thought to consist of an array of phase-variable polysaccharides that give rise to subpopulations with distinct cell surface structures. Here, we report the serendipitous discovery of a previously unknown surface structure in Bacteroides thetaiotaomicron: a surface layer composed of a protein of unknown function, BT1927. BT1927, which … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
16
0

Year Published

2018
2018
2024
2024

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 18 publications
(17 citation statements)
references
References 38 publications
1
16
0
Order By: Relevance
“…5c ). Three of these repeats are identical to those that mediate recombination of the BT1927 promoter 30 and the remaining 4 only vary by a trinucleotide in the middle of each imperfect palindrome ( Fig. 5c ).…”
Section: Resultsmentioning
confidence: 98%
See 1 more Smart Citation
“…5c ). Three of these repeats are identical to those that mediate recombination of the BT1927 promoter 30 and the remaining 4 only vary by a trinucleotide in the middle of each imperfect palindrome ( Fig. 5c ).…”
Section: Resultsmentioning
confidence: 98%
“…An additional 17 up-regulated genes belong to 8 loci that encode predicted outer membrane S-layer lipoproteins and OmpA β-barrel proteins. One of these (BT1927) was previously found to be phase-variable and increase B. thetaiotaomicron resistance to complement-mediated killing when locked in the “on” state 30 . The remaining S-layer clusters share both syntenic organization and weak homology to BT1927–25.…”
Section: Resultsmentioning
confidence: 99%
“…The modular nature of Type I specificity proteins allows the protein to change its recognition site by varying the N- and C-terminal TRD. Such domain shuffling and rearrangements of specificity-encoding genes has been demonstrated in numerous bacteria, and, in a few organisms, the shuffling is due to site-specific DNA inversions ( 11 , 16–19 ).…”
Section: Introductionmentioning
confidence: 99%
“…In the haloarchaeon Haloquadratum walsbyi DSM 16790, two different genomic islands encode glycosyltransferases and S-layer glycoproteins [ 70 ]. Thus, viruses may exert an influence that is comparable to host immune system, producing not just different surface types, analogous to serotypes in bacterial pathogens but also a mechanism of switching the from one surface type to another as often seen in human pathogens and commensals [ 71 , 72 ].…”
Section: Discussionmentioning
confidence: 99%