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Gene Review

sipA  -  cell invasion protein SipA

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

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Disease relevance of sipA

  • Infection of bovine ligated loops with the Salmonella enterica serotype Typhimurium wild type but not a sipA sopABDE2 mutant resulted in fluid accumulation, polymorphonuclear cell infiltration, and expression of CXC chemokines, particularly GRO alpha [1].
  • We found that sipA, sopE, and, to a lesser degree, sopE2 contribute to murine colitis, but we could not assign an inflammation phenotype to sopB [2].

High impact information on sipA

  • In contrast, mutations in sipA and sptP, which also encode secreted proteins, did not interfere with the translocation of SipC, indicating that only a subset of targets of the type III secretion system act as translocases [3].
  • Here we have revisited the question of which T3SS-1 effectors contribute to the invasion of epithelial cells by complementing a strain lacking all of the effector genes that are required to cause diarrhea in a calf (a sipA sopABDE2 mutant) [4].
  • A wild-type pattern of invasion was restored to the sipA mutant after the introduction of sipA on a plasmid [5].
  • A sipA mutant was impaired for invasion using a polarized cell line, but fully invasive in a non-polarized cell line [6].
  • It was the aim of the present study to characterize the interactions of a porcine Salmonella Typhimurium field strain and its isogenic mutants in the SPI-1 genes hilA, sipA and sipB with porcine macrophages [7].

Biological context of sipA


Analytical, diagnostic and therapeutic context of sipA

  • Time-lapse phase-contrast microscopy of membrane ruffle propagation in live cells confirmed that the sipA mutant induced membrane ruffles as efficiently as the wild-type bacteria [5].
  • Confocal microscopy of F-actin in tetramethyl rhodamine isothiocyanate (TRITC)-phalloidin-stained MDCK cells revealed no difference in either the frequency or the morphology of membrane ruffles induced by wild-type and sipA mutant strains of S. typhimurium [5].


  1. Secreted effector proteins of Salmonella enterica serotype typhimurium elicit host-specific chemokine profiles in animal models of typhoid fever and enterocolitis. Zhang, S., Adams, L.G., Nunes, J., Khare, S., Tsolis, R.M., Bäumler, A.J. Infect. Immun. (2003) [Pubmed]
  2. Role of the Salmonella pathogenicity island 1 effector proteins SipA, SopB, SopE, and SopE2 in Salmonella enterica subspecies 1 serovar Typhimurium colitis in streptomycin-pretreated mice. Hapfelmeier, S., Ehrbar, K., Stecher, B., Barthel, M., Kremer, M., Hardt, W.D. Infect. Immun. (2004) [Pubmed]
  3. The invasion-associated type III system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell. Collazo, C.M., Galán, J.E. Mol. Microbiol. (1997) [Pubmed]
  4. SipA, SopA, SopB, SopD, and SopE2 contribute to Salmonella enterica serotype typhimurium invasion of epithelial cells. Raffatellu, M., Wilson, R.P., Chessa, D., Andrews-Polymenis, H., Tran, Q.T., Lawhon, S., Khare, S., Adams, L.G., Bäumler, A.J. Infect. Immun. (2005) [Pubmed]
  5. Role of sipA in the early stages of Salmonella typhimurium entry into epithelial cells. Jepson, M.A., Kenny, B., Leard, A.D. Cell. Microbiol. (2001) [Pubmed]
  6. Salmonella Typhimurium SPI-1 genes promote intestinal but not tonsillar colonization in pigs. Boyen, F., Pasmans, F., Van Immerseel, F., Morgan, E., Adriaensen, C., Hernalsteens, J.P., Decostere, A., Ducatelle, R., Haesebrouck, F. Microbes Infect. (2006) [Pubmed]
  7. Role of SPI-1 in the interactions of Salmonella Typhimurium with porcine macrophages. Boyen, F., Pasmans, F., Donné, E., Van Immerseel, F., Adriaensen, C., Hernalsteens, J.P., Ducatelle, R., Haesebrouck, F. Vet. Microbiol. (2006) [Pubmed]
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