Peptidoglycan structure of <i>Salmonella typhimurium</i> growing within cultured mammalian cells

Jc, Quintela; Ma, de Pedro; Zöllner, Peter; Allmaier, Günter; F, Garcia-del Portillo

doi:10.1046/j.1365-2958.1997.2561621.x

Cited by 69 publications

(65 citation statements)

References 38 publications

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“…Thus, one possible biological role common for STM3117-3119 is to synthesize and modify the peptidoglycan layer, a major component of STM cell wall that serves as the first line of defense against the antibacterial regents produced by host cells (53). Consistent with this suggestion, prior measurements indicate that extensive peptidoglycan remodeling occurs following proliferation of STM within epithelial cells, and the peptidoglycan layer has been suggested to play an important role in mediating the infection of Salmonella (54,55). Furthermore, the composition of the peptidoglycan cell wall modulates the assembly and function of T3S (56).…”

Section: Discussionsupporting

confidence: 67%

Proteomic Analysis of Salmonella enterica Serovar Typhimurium Isolated from RAW 264.7 Macrophages

Shi

Adkins

Coleman

et al. 2006

Journal of Biological Chemistry

137

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To evade host resistance mechanisms, Salmonella enterica serovar Typhimurium (STM), a facultative intracellular pathogen, must alter its proteome following macrophage infection. To identify new colonization and virulence factors that mediate STM pathogenesis, we have isolated STM cells from RAW 264.7 macrophages at various time points following infection and used a liquid chromatography-mass spectrometry-based proteomic approach to detect the changes in STM protein abundance. Because host resistance to STM infection is strongly modulated by the expression of a functional host-resistant regulator, i.e. natural resistanceassociated macrophage protein 1 (Nramp1, also called Slc11a1), we have also examined the effects of Nramp1 activity on the changes of STM protein abundances. A total of 315 STM proteins have been identified from isolated STM cells, which are largely housekeeping proteins whose abundances remain relatively constant during the time course of infection. However, 39 STM proteins are strongly induced after infection, suggesting their involvement in modulating colonization and infection. Of the 39 induced proteins, 6 proteins are specifically modulated by Nramp1 activity, including STM3117, as well as STM3118 -3119 whose time-dependent abundance changes were confirmed using Western blot analysis. Deletion of the gene encoding STM3117 resulted in a dramatic reduction in the ability of STM to colonize wild-type RAW 264.7 macrophages, demonstrating a critical involvement of STM3117 in promoting the replication of STM inside macrophages. The predicted function common for STM3117-3119 is biosynthesis and modification of the peptidoglycan layer of the STM cell wall.

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Section: Discussionsupporting

confidence: 67%

Proteomic Analysis of Salmonella enterica Serovar Typhimurium Isolated from RAW 264.7 Macrophages

Shi

Adkins

Coleman

et al. 2006

Journal of Biological Chemistry

137

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“…These results indicate that the bacterial cell envelope is an important determinant for the establishment of a bacterium-host interaction. In line with this, it was observed that Salmonella enterica serovar Typhimurium peptidoglycan undergoes structural alterations that probably add to its fitness when it resides in mammalian cells (17,216).…”

Section: Genes Involved In Cell Envelope Structure and Modificationmentioning

confidence: 49%

Unraveling the Secret Lives of Bacteria: Use of In Vivo Expression Technology and Differential Fluorescence Induction Promoter Traps as Tools for Exploring Niche-Specific Gene Expression

Rediers

Rainey

Vanderleyden

et al. 2005

Microbiol Mol Biol Rev

140

120

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A major challenge for microbiologists is to elucidate the strategies deployed by microorganisms to adapt to and thrive in highly complex and dynamic environments. In vitro studies, including those monitoring genomewide changes, have proven their value, but they can, at best, mimic only a subset of the ensemble of abiotic and biotic stimuli that microorganisms experience in their natural habitats. The widely used gene-to-phenotype approach involves the identification of altered niche-related phenotypes on the basis of gene inactivation. However, many traits contributing to ecological performance that, upon inactivation, result in only subtle or difficult to score phenotypic changes are likely to be overlooked by this otherwise powerful approach. Based on the premise that many, if not most, of the corresponding genes will be induced or upregulated in the environment under study, ecologically significant genes can alternatively be traced using the promoter trap techniques differential fluorescence induction and in vivo expression technology (IVET). The potential and limitations are discussed for the different IVET selection strategies and system-specific variants thereof. Based on a compendium of genes that have emerged from these promoter-trapping studies, several functional groups have been distinguished, and their physiological relevance is illustrated with follow-up studies of selected genes. In addition to confirming results from largely complementary approaches such as signature-tagged mutagenesis, some unexpected parallels as well as distinguishing features of microbial phenotypic acclimation in diverse environmental niches have surfaced. On the other hand, by the identification of a large proportion of genes with unknown function, these promoter-trapping studies underscore how little we know about the secret lives of bacteria and other microorganisms

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“…2A). BLP and PGN are abundantly produced by all bacteria and are important PAMPs in bacterial-mediated diseases, including salmonellosis (46,47). It is unclear at present why galectin-3 selectively modulates some but not all TLR agonists' function.…”

Section: Discussionmentioning

confidence: 99%

Galectin-3 Is a Negative Regulator of Lipopolysaccharide-Mediated Inflammation

Komai-Koma

Gilchrist

et al. 2008

The Journal of Immunology

143

114

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Galectin-3 is a β-galactoside-binding lectin that plays an important role in inflammatory diseases. It also interacts with the surface carbohydrates of many pathogens, including LPS. However, its role in infection is not fully understood. Data presented herein demonstrate for the first time that galectin-3 is a negative regulator of LPS-induced inflammation. Galectin-3 is constitutively produced by macrophages and directly binds to LPS. Galectin-3-deficient macrophages had markedly elevated LPS-induced signaling and inflammatory cytokine production compared with wild-type cells, which was specifically inhibited by the addition of recombinant galectin-3 protein. In contrast, blocking galectin-3 binding sites by using a neutralizing Ab or its ligand, β-lactose, enhanced LPS-induced inflammatory cytokine expression by wild-type macrophages. In vivo, mice lacking galectin-3 were more susceptible to LPS shock associated with excessive induction of inflammatory cytokines and NO production. However, these changes conferred greater resistance to Salmonella infection. Thus, galectin-3 is a previously unrecognized, naturally occurring, negative regulator of LPS function, which protects the host from endotoxin shock but, conversely, favors Salmonella survival.

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Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells

Cited by 69 publications

References 38 publications

Proteomic Analysis of Salmonella enterica Serovar Typhimurium Isolated from RAW 264.7 Macrophages

Proteomic Analysis of Salmonella enterica Serovar Typhimurium Isolated from RAW 264.7 Macrophages

Unraveling the Secret Lives of Bacteria: Use of In Vivo Expression Technology and Differential Fluorescence Induction Promoter Traps as Tools for Exploring Niche-Specific Gene Expression

Galectin-3 Is a Negative Regulator of Lipopolysaccharide-Mediated Inflammation

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