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

Kim, Hyeon Guk; Kim, Bae Hoon; Kim, Jin Seok; Eom, Joong Sik; Bang, Iel Soo; Bang, Seong Ho; Lee, In Su; Park, Yong Keun

doi:10.1099/mic.0.2007/011528-0

Cited by 5 publications

(6 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Surface display of a heterologous antigen can induce antigen‐specific local and systemic immune responses after oral administration of attenuated S. Typhimurium (13). A peptide representing the first 160 amino acids of SipB is reportedly localized on the bacterial cell surface after secretion and amino acids 120–140 are required for this localization (12). To investigate whether TTFC fused to the SipB T3SS signal is displayed on the bacterial surface, we performed subcellular fractionation of S .…”

Section: Resultsmentioning

confidence: 99%

“…Typhimurium (24, 25). Plasmid pYKJ357 expresses the SipB secretion signal (residues 1–40) but lacks the domain required for outer membrane localization (residues 120–140) (12). As shown in Figure 5, TTFC proteins fused to a delivery signal are expressed from both pYKJ356 and pYKJ357; however, the amount of secretion of TTFC was higher with T3SS‐mediated than with beta‐lactamase secretion.…”

Section: Resultsmentioning

confidence: 99%

“…Subcellular fractionation of S. Typhimurium was performed as described previously (12). Briefly, bacterial cultures grown in LB broth containing 0.3 M NaCl were centrifuged at 8000 g for 10 mins.…”

Section: Methodsmentioning

confidence: 99%

“…S. Typhimurium possesses two T3SSs encoded by Salmonella pathogenicity islands (SPIs) 1 and 2; SPI‐1 is required for invasion of non‐phagocytic epithelial cells and SPI‐2 for replication and survival in macrophages (4). In previous studies, we showed that a Listeria monocytogenes antigen (LLO) fused to the N‐terminal 160 amino acids of T3SS translocon protein SipB is secreted into the culture supernatant and transiently localized on the bacterial surface (11, 12). Since display of foreign antigens on the surface of attenuated Salmonella strains enhances an immunostimulatory effect (13,14), the SipB N‐terminus can be utilized for heterologous antigen delivery, thereby increasing antigen presentation by APCs.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Expression and delivery of tetanus toxin fragment C fused to the N‐terminal domain of SipB enhances specific immune responses in mice

Jang

Kim

Eom

et al. 2012

Microbiology and Immunology

Self Cite

View full text Add to dashboard Cite

Live attenuated bacteria can be used as a carrier for the delivery of foreign antigens to a host's immune system. The N‐terminal domain of SipB, a translocon protein of the type III secretion system of Salmonella enterica serovar Typhimurium, is required for secretion and outer membrane localization. In the present study, vaccine plasmids for antigen delivery in which the non‐toxic tetanus toxin fragment C (TTFC), which contains a T cell epitope, is fused to the N‐terminal 160 amino acids of SipB were developed. It was found that the recombinant proteins are secreted into the culture media and localized to the bacterial surface. TTFC‐specific antibody responses are significantly increased in mice orally immunized with attenuated S. Typhimurium BRD509 strains carrying TTFC delivery plasmids. When the TTFC delivery cassettes were introduced into a low copy vector, the plasmid was stably maintained in the BRD509 strain and induced an immune response to the TTFC antigen in mice. These results suggest that expression and delivery of heterologous antigens fused to the N‐terminus of SipB enhance the induction of antigen‐specific immune responses, and that the N‐terminal domain of SipB can be used as a versatile delivery system for foreign antigens.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Expression and delivery of tetanus toxin fragment C fused to the N‐terminal domain of SipB enhances specific immune responses in mice

Jang

Kim

Eom

et al. 2012

Microbiology and Immunology

Self Cite

View full text Add to dashboard Cite

show abstract

“…For the activation of the T3SS-related genes, Salmonella serovar Typhimurium bacteria were grown under the growth conditions described above for 3 h. Membrane proteins of Salmonella serovar Typhimurium were prepared as previously described (29). Briefly, isolated whole membranes were placed onto a six-step sucrose gradient, centrifuged at 100,000 ϫ g for 36 h, and then divided into 14 fractions.…”

Section: Methodsmentioning

confidence: 99%

Role of Salmonella Pathogenicity Island 1 Protein IacP in Salmonella enterica Serovar Typhimurium Pathogenesis

et al. 2011

Self Cite

View full text Add to dashboard Cite

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. When the iacP gene was deleted from several Salmonella serovar Typhimurium strains, the invasion into INT-407 epithelial cells was significantly decreased compared to that of their parental strains, and retarded rearrangements of actin fibers were observed for the iacP mutant-infected cells. Although IacP had no effect on the secretion of type III translocon proteins, the levels of secretion of the effector proteins SopB, SopA, and SopD into the culture medium were decreased in the iacP mutant. In a mouse infection model, mice infected with the iacP mutant exhibited alleviated pathological signs in the intestine and survived longer than did wild-type-infected mice. Taken together, IacP plays a key role in Salmonella virulence by regulating the translocation of T3SS effector proteins.

show abstract

Deletion of Invasion Protein B in Salmonella enterica Serovar Typhimurium Influences Bacterial Invasion and Virulence

et al. 2015

View full text Add to dashboard Cite

Salmonella enterica serovar Typhimurium (S. Typhimurium) has a wide host range and causes infections ranging from severe gastroenteritis to systemic infections in human, as well as causing typhoid-like disease in murine models of infection. S. Typhimurium translocates its effector proteins through the Salmonella pathogenicity island-I (SPI-I)-encoded T3SS-I needle complex. This study focuses on invasion protein B (SipB) of S. Typhimurium, which plays an active role in SPI-I invasion efficiency. To test our hypothesis, a sipB deletion mutant was constructed through double-crossover allelic using the suicide vector pRE112ΔsipB, and its biological characteristics were analyzed. The results showed that the SipB does not affect the growth of Salmonella, but the adherence, invasion, and virulence of the mutant were significantly decreased compared with wild-type S. Typhimurium (SL1344). This research indicates that SipB is an important virulence factor in the pathogenicity of S. Typhimurium.

show abstract

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

Cited by 5 publications

References 42 publications

Expression and delivery of tetanus toxin fragment C fused to the N‐terminal domain of SipB enhances specific immune responses in mice

Expression and delivery of tetanus toxin fragment C fused to the N‐terminal domain of SipB enhances specific immune responses in mice

Role of Salmonella Pathogenicity Island 1 Protein IacP in Salmonella enterica Serovar Typhimurium Pathogenesis

Deletion of Invasion Protein B in Salmonella enterica Serovar Typhimurium Influences Bacterial Invasion and Virulence

Contact Info

Product

Resources

About