PMID- 25153529
OWN - NLM
STAT- MEDLINE
DCOM- 20151218
LR  - 20211021
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 9
IP  - 8
DP  - 2014
TI  - Modulation of biofilm-formation in Salmonella enterica serovar Typhimurium by the 
      periplasmic DsbA/DsbB oxidoreductase system requires the GGDEF-EAL domain protein 
      STM3615.
PG  - e106095
LID - 10.1371/journal.pone.0106095 [doi]
LID - e106095
AB  - In Salmonella enterica serovar Typhimurium (S. Typhimurium), biofilm-formation is 
      controlled by the cytoplasmic intracellular small-molecular second messenger 
      cyclic 3', 5'-di- guanosine monophosphate (c-di-GMP) through the activities of 
      GGDEF and EAL domain proteins. Here we describe that deleting either dsbA or 
      dsbB, respectively encoding a periplasmic protein disulfide oxidase and a 
      cytoplasmic membrane disulfide oxidoreductase, resulted in increased 
      biofilm-formation on solid medium. This increased biofilm-formation, defined as a 
      red, dry and rough (rdar) colony morphotype, paralleled with enhanced expression 
      of the biofilm master regulator CsgD and the biofilm-associated fimbrial subunit 
      CsgA. Deleting csgD in either dsb mutant abrogated the enhanced 
      biofilm-formation. Likewise, overexpression of the c-di-GMP phosphodiesterase 
      YhjH, or mutationally inactivating the CsgD activator EAL-domain protein YdiV, 
      reduced biofilm-formation in either of the dsb mutants. Intriguingly, deleting 
      the GGDEF-EAL domain protein gene STM3615 (yhjK), previously not connected to 
      rdar morphotype development, also abrogated the escalated rdar morphotype 
      formation in dsb mutant backgrounds. Enhanced biofilm-formation in dsb mutants 
      was furthermore annulled by exposure to the protein disulfide catalyst copper 
      chloride. When analyzed for the effect of exogenous reducing stress on 
      biofilm-formation, both dsb mutants initially showed an escalated rdar morphotype 
      development that later dissolved to reveal a smooth mucoid colony morphotype. 
      From these results we conclude that biofilm-development in S. Typhimurium is 
      affected by periplasmic protein disulphide bond status through CsgD, and discuss 
      the involvement of selected GGDEF/EAL domain protein(s) as signaling mediators.
FAU - Anwar, Naeem
AU  - Anwar N
AD  - Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 
      Stockholm, Sweden; Department of Biology, Syed Babar Ali School of Science and 
      Engineering, Lahore University of Management Sciences, Lahore, Pakistan.
FAU - Rouf, Syed Fazle
AU  - Rouf SF
AD  - Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 
      Stockholm, Sweden.
FAU - Romling, Ute
AU  - Romling U
AD  - Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 
      Stockholm, Sweden.
FAU - Rhen, Mikael
AU  - Rhen M
AD  - Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 
      Stockholm, Sweden.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140825
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (Bacterial Proteins)
RN  - 0 (DsbB protein, Bacteria)
RN  - 0 (Membrane Proteins)
RN  - 0 (Periplasmic Proteins)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.8.4.- (periplasmic protein disulfide oxidoreductase)
RN  - EC 5.3.4.1 (Protein Disulfide-Isomerases)
RN  - H2D2X058MU (Cyclic GMP)
SB  - IM
MH  - Bacterial Proteins/genetics/*metabolism
MH  - Biofilms/*growth & development
MH  - Cyclic GMP/metabolism
MH  - Gene Expression Regulation, Bacterial/genetics
MH  - Membrane Proteins/genetics/*metabolism
MH  - Oxidoreductases/genetics/*metabolism
MH  - Periplasmic Proteins/genetics/*metabolism
MH  - Protein Disulfide-Isomerases/genetics/*metabolism
MH  - Protein Structure, Tertiary/*genetics
MH  - Salmonella typhimurium/genetics/*metabolism
PMC - PMC4143323
COIS- Competing Interests: The authors have declared that no competing interests exist.
EDAT- 2014/08/26 06:00
MHDA- 2015/12/19 06:00
PMCR- 2014/08/25
CRDT- 2014/08/26 06:00
PHST- 2014/04/17 00:00 [received]
PHST- 2014/08/01 00:00 [accepted]
PHST- 2014/08/26 06:00 [entrez]
PHST- 2014/08/26 06:00 [pubmed]
PHST- 2015/12/19 06:00 [medline]
PHST- 2014/08/25 00:00 [pmc-release]
AID - PONE-D-14-17413 [pii]
AID - 10.1371/journal.pone.0106095 [doi]
PST - epublish
SO  - PLoS One. 2014 Aug 25;9(8):e106095. doi: 10.1371/journal.pone.0106095. 
      eCollection 2014.