ABI domain‐containing proteins contribute to surface protein display and cell division in <i>Staphylococcus aureus</i>

Frankel, Matthew; Wojcik, Brandon M.; DeDent, Andrea C.; Missiakas, Dominique; Schneewind, Olaf

doi:10.1111/j.1365-2958.2010.07334.x

Cited by 40 publications

(49 citation statements)

References 73 publications

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“…Three other genes in the WTA interaction network (lyrA, 965, and SAOUHSC_02256) encode structurally related membrane proteins that resemble type II CAAX prenyl endopeptidases, a family of proteins well known in eukaryotes because key members are involved in the proteolytic processing of prenylated Ras and other lipoproteins (30). There are five genes encoding CAAX protease-like (CPL) homologs in S. aureus, including the three identified in the growth depletion analysis, but only ΔlyrA mutants have been characterized (31,32). These mutants have altered crosswall structures and are deficient in a subset of surface proteins, but as yet there is no evidence that LyrA has a proteolytic function.…”

Section: Linkage Analysis Provided Gene-gene Validation Of Compound-genementioning

confidence: 99%

Compound-gene interaction mapping reveals distinct roles forStaphylococcus aureusteichoic acids

Maria

Sadaka

Moussa

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Staphylococcus aureus contains two distinct teichoic acid (TA) polymers, lipoteichoic acid (LTA) and wall teichoic acid (WTA), which are proposed to play redundant roles in regulating cell division. To gain insight into the underlying biology of S. aureus TAs, we used a small molecule inhibitor to screen a highly saturated transposon library for cellular factors that become essential when WTA is depleted. We constructed an interaction network connecting WTAs with genes involved in LTA synthesis, peptidoglycan synthesis, surface protein display, and D-alanine cell envelope modifications. Although LTAs and WTAs are synthetically lethal, we report that they do not have the same synthetic interactions with other cell envelope genes. For example, D-alanylation, a tailoring modification of both WTAs and LTAs, becomes essential when the former, but not the latter, are removed. Therefore, D-alanine-tailored LTAs are required for survival when WTAs are absent. Examination of terminal phenotoypes led to the unexpected discovery that cells lacking both LTAs and WTAs lose their ability to form Z rings and can no longer divide. We have concluded that the presence of either LTAs or WTAs on the cell surface is required for initiation of S. aureus cell division, but these polymers act as part of distinct cellular networks.synthetic lethality | TraDIS | Tn-seq

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Section: Linkage Analysis Provided Gene-gene Validation Of Compound-genementioning

confidence: 99%

Compound-gene interaction mapping reveals distinct roles forStaphylococcus aureusteichoic acids

Maria

Sadaka

Moussa

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…Bacterial lysates and supernatants were prepared as described previously (27), with modifications. Please refer to the supplemental material for details.…”

Section: Methodsmentioning

confidence: 99%

Staphylococcal Esx Proteins Modulate Apoptosis and Release of Intracellular Staphylococcus aureus during Infection in Epithelial Cells

et al. 2014

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bThe opportunistic pathogen Staphylococcus aureus is one of the major causes of health care-associated infections. S. aureus is primarily an extracellular pathogen, but it was recently reported to invade and replicate in several host cell types. The ability of S. aureus to persist within cells has been implicated in resistance to antimicrobials and recurrent infections. However, few staphylococcal proteins that mediate intracellular survival have been identified. Here we examine if EsxA and EsxB, substrates of the ESAT-6-like secretion system (Ess), are important during intracellular S. aureus infection. The Esx proteins are required for staphylococcal virulence, but their functions during infection are unclear. While isogenic S. aureus esxA and esxB mutants were not defective for epithelial cell invasion in vitro, a significant increase in early/late apoptosis was observed in esxA mutant-infected cells compared to wild-type-infected cells. Impeding secretion of EsxA by deleting C-terminal residues of the protein also resulted in a significant increase of epithelial cell apoptosis. Furthermore, cells transfected with esxA showed an increased protection from apoptotic cell death. A double mutant lacking both EsxA and EsxB also induced increased apoptosis but, remarkably, was unable to escape from cells as efficiently as the single mutants or the wild type. Thus, using in vitro models of intracellular staphylococcal infection, we demonstrate that EsxA interferes with host cell apoptotic pathways and, together with EsxB, mediates the release of S. aureus from the host cell.

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“…The exact mechanism by which PncO regulates bacteriocin production or mediates immunity is currently unknown. CPBP proteins have also been shown to be involved in the expression of surface proteins containing the YSIRK signal peptide, as in the case of Staphylococcus aureus Spd proteins (73). Recently, Firon and colleagues have shown that in S. agalactiae, a CPBP protein, Abx, forms a signaling complex with the histidine kinase CovS and regulates expression of virulence factors (74).…”

Section: Discussionmentioning

confidence: 99%

A Conserved Streptococcal Membrane Protein, LsrS, Exhibits a Receptor-Like Function for Lantibiotics

Biswas

2014

J Bacteriol

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Streptococcus mutans strain GS-5 produces a two-peptide lantibiotic, Smb, which displays inhibitory activity against a broad spectrum of bacteria, including other streptococci. For inhibition, lantibiotics must recognize specific receptor molecules present on the sensitive bacterial cells. However, so far no such receptor proteins have been identified for any lantibiotics. In this study, using a powerful transposon mutagenesis approach, we have identified in Streptococcus pyogenes a gene that exhibits a receptor-like function for Smb. The protein encoded by that gene, which we named LsrS, is a membrane protein belonging to the CAAX protease family. We also found that nisin, a monopeptide lantibiotic, requires LsrS for its optimum inhibitory activity. However, we found that LsrS is not required for inhibition by haloduracin and galolacticin, both of which are two-peptide lantibiotics closely related to Smb. LsrS appears to be a well-conserved protein that is present in many streptococci, including S. mutans. Inactivation of SMU.662, an LsrS homolog, in S. mutans strains UA159 and V403 rendered the cells refractory to Smbmediated killing. Furthermore, overexpression of LsrS in S. mutans created cells more susceptible to Smb. Although LsrS and its homolog contain the CAAX protease domain, we demonstrate that inactivation of the putative active sites on the LsrS protein has no effect on its receptor-like function. This is the first report describing a highly conserved membrane protein that displays a receptor-like function for lantibiotics.

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ABI domain‐containing proteins contribute to surface protein display and cell division in Staphylococcus aureus

Cited by 40 publications

References 73 publications

Compound-gene interaction mapping reveals distinct roles forStaphylococcus aureusteichoic acids

Compound-gene interaction mapping reveals distinct roles forStaphylococcus aureusteichoic acids

Staphylococcal Esx Proteins Modulate Apoptosis and Release of Intracellular Staphylococcus aureus during Infection in Epithelial Cells

A Conserved Streptococcal Membrane Protein, LsrS, Exhibits a Receptor-Like Function for Lantibiotics

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