Anti plague Research Institute

Rostov-na-Donu, Russia

Anti plague Research Institute

Rostov-na-Donu, Russia

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Podladchikova O.,Anti plague Research Institute | Antonenka U.,Max Von Pettenkofer Institute | Heesemann J.,Max Von Pettenkofer Institute | Rakin A.,Max Von Pettenkofer Institute
International Journal of Medical Microbiology | Year: 2011

Autoagglutination (AA) is a protective phenotypic trait facilitating survival of bacteria in hostile environments and in the host during infection. Autoagglutination factors (AFs) that possess self-associating ability are currently characterized in many Gram-negative bacteria, but Yersinia pestis AFs are still a matter of debate. Previously, we have shown that AF of Hms - strain Y. pestis EV76 is a complex of the 17,485-kDa protein and a low-molecular-weight component with siderophore activity. Here, we identified the protein moiety of AF and examined its role in AA of Hms + and Hms - Y. pestis strains. Using MALDI-TOF MS of trypsin-hydrolyzed AF, we unambiguously identified the protein as YPO0502, which belongs to a family of Hcp-proteins forming pilus-like structures of the type six secretion system (T6SS). To address the role of YPO0502 in AA, we cloned ypo0502 in E. coli, overexpressed it in Y. pestis and constructed its knock-out mutant in Y. pestis. However, all these approaches failed: YPO0502 was not secreted in E. coli, formed inclusion bodies when overexpressed in Y. pestis, and could probably be compensated by other Hcp-like proteins in Y. pestis. In contrast, downregulation of ypo0502 expression by its antisense RNA supported the contribution of YPO0502 in AA of Hms + and Hms - Y. pestis strains. The results of the present study indicate that the Hcp-like component of T6SS encoded by ypo502 is involved in Y. pestis AA and suggest that at least one (ypo0499-0516) of the 6 T6SS clusters of Y. pestis is involved in bacterial interaction. © 2011 Elsevier GmbH.


Podladchikova O.,Anti plague Research Institute | Rykova V.,Anti plague Research Institute | Antonenka U.,Max Von Pettenkofer Institute | Rakin A.,Max Von Pettenkofer Institute
Advances in Experimental Medicine and Biology | Year: 2012

Autoagglutination (AA) is a virulence-associated trait typical of various pathogenic bacteria, including Yersinia pestis. In this study, we show that AA in Y. pestis is a complex phenomenon determined by the HCP-like protein of T6SS which is encoded by ypo0502 and by the siderophore Yersiniachelin (Ych) which is encoded by the ysu locus. Down-regulation of YPO0502 expression by antisense RNA abrogates AA in G8786 (Hms+) and EV76 (Hms-) Y. pestis strains. The deletion of Ych biosynthetic genes ypo1530-1532 in EV76 though does not abolish AA results in its noticeable depression. © 2012 Springer Science+Business Media New York.


PubMed | Anti plague Research Institute
Type: Journal Article | Journal: International journal of medical microbiology : IJMM | Year: 2011

Autoagglutination (AA) is a protective phenotypic trait facilitating survival of bacteria in hostile environments and in the host during infection. Autoagglutination factors (AFs) that possess self-associating ability are currently characterized in many Gram-negative bacteria, but Yersinia pestis AFs are still a matter of debate. Previously, we have shown that AF of Hms(-) strain Y. pestis EV76 is a complex of the 17,485-kDa protein and a low-molecular-weight component with siderophore activity. Here, we identified the protein moiety of AF and examined its role in AA of Hms(+) and Hms(-)Y. pestis strains. Using MALDI-TOF MS of trypsin-hydrolyzed AF, we unambiguously identified the protein as YPO0502, which belongs to a family of Hcp-proteins forming pilus-like structures of the type six secretion system (T6SS). To address the role of YPO0502 in AA, we cloned ypo0502 in E. coli, overexpressed it in Y. pestis and constructed its knock-out mutant in Y. pestis. However, all these approaches failed: YPO0502 was not secreted in E. coli, formed inclusion bodies when overexpressed in Y. pestis, and could probably be compensated by other Hcp-like proteins in Y. pestis. In contrast, downregulation of ypo0502 expression by its antisense RNA supported the contribution of YPO0502 in AA of Hms(+) and Hms(-)Y. pestis strains. The results of the present study indicate that the Hcp-like component of T6SS encoded by ypo502 is involved in Y. pestis AA and suggest that at least one (ypo0499-0516) of the 6 T6SS clusters of Y. pestis is involved in bacterial interaction.

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