Molecular characterization of the InvE regulator in the secretion of type III secretion translocases in Salmonella enterica serovar Typhimurium.

The type III secretion systems (T3SSs) are exploited by many Gram-negative pathogenic bacteria to deliver a set of effector proteins into the host cytosol during cell entry. The T3SS of Salmonella enterica serovar Typhimurium is composed of more than 20 proteins that constitute the membrane-associated base, the needle and the tip complex at the distal end of the T3SS needle. Membrane docking and piercing between the T3SS and host cells is followed by the secretion of effector proteins.

A phosphotransferase system permease is a novel component of CadC signaling in Salmonella enterica.

In Salmonella enterica serovar Typhimurium, proteolytic cleavage of the membrane-bound transcriptional regulator CadC acts as a switch to activate genes of the lysine decarboxylase system in response to low pH and lysine signals. To identify the genetic factors required for the proteolytic activation of CadC, we performed genome-wide random mutagenesis. We show that a phosphotransferase system (PTS) permease STM4538 acts as a positive modulator of CadC function.

Role of Salmonella Pathogenicity Island 1 protein IacP in Salmonella enterica serovar typhimurium pathogenesis.

Gram-negative bacteria, including Salmonella enterica serovar Typhimurium, exploit type III secretion systems (T3SSs) through which virulence proteins are delivered into the host cytosol to reinforce invasive and replicative niches in their host. Although many secreted effector proteins and membrane-bound structural proteins in the T3SS have been characterized, the functions of many cytoplasmic proteins still remain unknown. In this study, we found that IacP, encoded by Salmonella pathogenicity island 1, was important for nonphagocytic cell invasion and bacterial virulence.

N-terminal residues of SipB are required for its surface localization on Salmonella enterica serovar Typhimurium.

SipB, one of the invasion proteins encoded in Salmonella pathogenicity island 1 (SPI-1), is known to be secreted outside the cell, where it functions as a translocon by assembling into a host-cell plasma membrane-integral structure. Here, we confirmed that wild-type SipB could be localized to the bacterial outer membrane, and further showed that its localization was dependent on extracellular secretion, and was independent of the presence of the SipD protein. Proteinase K susceptibility and immunofluorescence assays indicated that SipB was not incorporated into the outer membrane, but rather was displayed on the bacterial surface.

CadC has a global translational effect during acid adaptation in Salmonella enterica serovar Typhimurium.

In Salmonella enterica serovar Typhimurium, the membrane-localized CadC is a transcriptional activator of the cadBA operon, which contributes to the acid tolerance response. Unlike in Escherichia coli, in which transcription of cadC is constitutive, in S. enterica serovar Typhimurium cadC expression is induced by low pH and lysine.