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YqiC of Salmonella enterica serovar Typhimurium is a membrane fusogenic protein required for mice colonization.

Carrica MC, Craig PO, García-Angulo VA, Aguirre A, García-Véscovi E, Goldbaum FA, Cravero SL - BMC Microbiol. (2011)

Bottom Line: We found that YqiC shares biophysical and biochemical properties with Brucella abortus BMFP, the only previously characterized member of this group, such as a high alpha helix content, a coiled-coil domain involved in trimerization and a membrane fusogenic activity in vitro.In addition, we demonstrated that YqiC localizes at cytoplasmic and membrane subcellular fractions, that a S.This work firstly demonstrates the importance of a COG2960 member for pathogen-host interaction, and suggests a common function conserved among members of this group.

View Article: PubMed Central - HTML - PubMed

Affiliation: Instituto de Biotecnología, CICVyA-INTA Castelar, Los Reseros y Las Cabañas s/n, Buenos Aires, Argentina. mcarrica@leloir.org.ar

ABSTRACT

Background: Salmonella enterica serovar Typhimurium is an intracellular bacterial pathogen which can colonize a variety of hosts, including human, causing syndromes that vary from gastroenteritis and diarrhea to systemic disease.

Results: In this work we present structural information as well as insights into the in vivo function of YqiC, a 99-residue protein of S. Typhimurium, which belongs to the cluster of the orthologous group 2960 (COG2960). We found that YqiC shares biophysical and biochemical properties with Brucella abortus BMFP, the only previously characterized member of this group, such as a high alpha helix content, a coiled-coil domain involved in trimerization and a membrane fusogenic activity in vitro. In addition, we demonstrated that YqiC localizes at cytoplasmic and membrane subcellular fractions, that a S. Typhimurium yqiC deficient strain had a severe attenuation in virulence in the murine model when inoculated both orally and intraperitoneally, and was impaired to replicate at physiological and high temperatures in vitro, although it was still able to invade and replicate inside epithelial and macrophages cell lines.

Conclusion: This work firstly demonstrates the importance of a COG2960 member for pathogen-host interaction, and suggests a common function conserved among members of this group.

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Far UV-CD spectrum of YqiC measured in 50 mM Tris-HCl, 150 mM NaCl buffer (pH 8.0).
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Figure 1: Far UV-CD spectrum of YqiC measured in 50 mM Tris-HCl, 150 mM NaCl buffer (pH 8.0).

Mentions: YqiC is a 99-residue protein of S. Typhimurium (UniProtKB entry K09806) which belongs to the cluster of orthologous groups 2960 (COG 2960). The bioinformatic analysis of the primary sequence of YqiC predicts a high helical content (66-77%) http://www.predictprotein.org, including two helical segments that span the N- and C-terminal halves of the protein (encompassing residues 4-43 and 49-79, respectively). Both helical segments are amphipathic but only the C-terminal one is predicted to form a coiled-coil structure http://groups.csail.mit.edu/cb/paircoil/paircoil.html. YqiC secondary structure was experimentally determined by its far UV circular dichroism spectrum (Figure 1), which showed a typical signature of an alpha helical protein. The percentage of helical structure of YqiC, estimated through the analysis of its CD spectra using K2D program (63%), agrees with the percentage of amino acids involved in the predicted N- and C-terminal alpha helices.


YqiC of Salmonella enterica serovar Typhimurium is a membrane fusogenic protein required for mice colonization.

Carrica MC, Craig PO, García-Angulo VA, Aguirre A, García-Véscovi E, Goldbaum FA, Cravero SL - BMC Microbiol. (2011)

Far UV-CD spectrum of YqiC measured in 50 mM Tris-HCl, 150 mM NaCl buffer (pH 8.0).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3107778&req=5

Figure 1: Far UV-CD spectrum of YqiC measured in 50 mM Tris-HCl, 150 mM NaCl buffer (pH 8.0).
Mentions: YqiC is a 99-residue protein of S. Typhimurium (UniProtKB entry K09806) which belongs to the cluster of orthologous groups 2960 (COG 2960). The bioinformatic analysis of the primary sequence of YqiC predicts a high helical content (66-77%) http://www.predictprotein.org, including two helical segments that span the N- and C-terminal halves of the protein (encompassing residues 4-43 and 49-79, respectively). Both helical segments are amphipathic but only the C-terminal one is predicted to form a coiled-coil structure http://groups.csail.mit.edu/cb/paircoil/paircoil.html. YqiC secondary structure was experimentally determined by its far UV circular dichroism spectrum (Figure 1), which showed a typical signature of an alpha helical protein. The percentage of helical structure of YqiC, estimated through the analysis of its CD spectra using K2D program (63%), agrees with the percentage of amino acids involved in the predicted N- and C-terminal alpha helices.

Bottom Line: We found that YqiC shares biophysical and biochemical properties with Brucella abortus BMFP, the only previously characterized member of this group, such as a high alpha helix content, a coiled-coil domain involved in trimerization and a membrane fusogenic activity in vitro.In addition, we demonstrated that YqiC localizes at cytoplasmic and membrane subcellular fractions, that a S.This work firstly demonstrates the importance of a COG2960 member for pathogen-host interaction, and suggests a common function conserved among members of this group.

View Article: PubMed Central - HTML - PubMed

Affiliation: Instituto de Biotecnología, CICVyA-INTA Castelar, Los Reseros y Las Cabañas s/n, Buenos Aires, Argentina. mcarrica@leloir.org.ar

ABSTRACT

Background: Salmonella enterica serovar Typhimurium is an intracellular bacterial pathogen which can colonize a variety of hosts, including human, causing syndromes that vary from gastroenteritis and diarrhea to systemic disease.

Results: In this work we present structural information as well as insights into the in vivo function of YqiC, a 99-residue protein of S. Typhimurium, which belongs to the cluster of the orthologous group 2960 (COG2960). We found that YqiC shares biophysical and biochemical properties with Brucella abortus BMFP, the only previously characterized member of this group, such as a high alpha helix content, a coiled-coil domain involved in trimerization and a membrane fusogenic activity in vitro. In addition, we demonstrated that YqiC localizes at cytoplasmic and membrane subcellular fractions, that a S. Typhimurium yqiC deficient strain had a severe attenuation in virulence in the murine model when inoculated both orally and intraperitoneally, and was impaired to replicate at physiological and high temperatures in vitro, although it was still able to invade and replicate inside epithelial and macrophages cell lines.

Conclusion: This work firstly demonstrates the importance of a COG2960 member for pathogen-host interaction, and suggests a common function conserved among members of this group.

Show MeSH
Related in: MedlinePlus