Disease relevance of invA

• We examined the functional conservation among members of this protein family by assessing the ability of MxiA of Shigella flexneri and LcrD of Yersinia pseudotuberculosis to restore invasiveness to an invA mutant of Salmonella typhimurium [1].
• Addition of EGF to cultured Henle-407 cells allowed the internalization of the invasion-defective S. typhimurium invA mutant although it did not cause the internalization of an adherent, but non-invasive, strain of Escherichia coli [2].
• Mutants defective for expression of invA, a component of Salmonella pathogenicity island 1 which is vital for efficient invasion of cultured cells, fail to induce FAE destruction and, when inoculated in LB, are attenuated for M-cell invasion [3].
• These data show that both the invA- and lpfC-mediated pathways of intestinal perforation are conserved in mouse virulent Salmonella serotypes [4].
• A protein of this size was visualized when invA was expressed in a bacteriophage T7 RNA polymerase-based expression system [5].

High impact information on invA

• In contrast, an isogenic strain of S. typhimurium that is defective in invasion owing to a mutation in the invA gene is unable to induce such phosphorylation [2].
• In contrast, three different S. typhimurium aroA strains and an invA mutant of SL1344 did not induce significant fluid accumulation in the rabbit ileal loops [6].
• Synergistic effect of mutations in invA and lpfC on the ability of Salmonella typhimurium to cause murine typhoid [4].
• During mixed-infection experiments, the S. typhimurium invA lpfC mutant showed a strong defect in colonizing Peyer's patches and mesenteric lymph nodes [4].
• In this study, we show that mutants possessing defects in one of two inv genes, invA or invG, which render them severely deficient for invasion of polarized epithelial MDCK cells, retain their ability to actively invade mouse Peyer's patch M cells [7].

Chemical compound and disease context of invA

• The use of digoxigenin (DIG) as a label provided greater sensitivity than biotin in a PCR system targeting the invA gene from Salmonella typhimurium [8].

Biological context of invA

• Transcriptional and translational cat and phoA fusions to invA (the proximal gene in the invABC operon) were constructed, and their expression was studied by measuring the levels of alkaline phosphatase or chloramphenicol acetyltransferase activity in mutants grown under different conditions [9].
• The invasion phenotype of invA mutants was readily rescued by wild-type S. typhimurium when cultured epithelial cells were simultaneously infected with both strains [5].
• The nucleotide sequence of invA showed an open reading frame capable of encoding a polypeptide of 686 amino acids with eight possible membrane-spanning regions and a predicted molecular weight of 75,974 [5].
• The invA locus was found to be located at about 59 min on the Salmonella chromosome, 7% linked to mutS [5].
• The degradation rates of DNA, both free and from dead Salmonella, were evaluated in natural seawaters maintained at 10 degrees and 20 degrees C, using PCR with Vir and invA primers [10].

Anatomical context of invA

• Nonpolar S. typhimurium invA mutants were deficient in invasion of cultured epithelial cells although they were fully capable of attaching to the same cells [5].

Associations of invA with chemical compounds

• Infection with either wild-type S. typhimurium, bacterial culture supernatant, or the noninvasive invA mutant was associated with induction of tyrosine phosphorylation of host cell mitogenic activating protein kinase [11].
• Strains grown in high-osmolarity media in the presence of subinhibitory concentrations of gyrase inhibitors (novobiocin or coumermycin A1), which reduce the level of DNA supercoiling, showed reduced expression of invA [9].
• A multiplex PCR method was developed to simultaneously amplify four genes, florfenicol (flo(st)), virulence (spvC), invasion (invA), and integron (int) from S. typhimurium DT104 (ACSSuT-type) [12].

Regulatory relationships of invA

• Nevertheless, invA was poorly expressed in topA mutants of S. typhimurium, which have increased DNA superhelicity [9].

Other interactions of invA

• The osmoinducibility of invA was independent of ompR, which controls the osmoinducibility of other genes [9].

Analytical, diagnostic and therapeutic context of invA

• Cultures were screened by inoculating a single colony of bacteria directly into a polymerase chain reaction (PCR) mixture which contained a pair of primers specific for the invA gene [13].

References