Phospholipid composition and phospholipase A activity of Neisseria gonorrhoeae

Senff, Leah M. M.; Wegener, Warner S.; Brooks, George F.; Finnerty, W. R.; Makula, R. A.

doi:10.1128/jb.127.2.874-880.1976

Cited by 42 publications

(20 citation statements)

References 34 publications

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“…The relative amounts of PE, PG, LPE and FFA in strains JW-31 and CS-7 were similar to those reported for other strains of N. gonorrhoeae (2,3,16). Other investigators (2,3,16) have reported that cardiolipin is present in gonococci in low concentrations (<2%). Using two dimensional TLC with n-butanol/acetic acid/water (60:20:20, v/v) as the second solvent (17), we could not detect [all]labeled cardiolipin in exponential phase cells of strains JW-31 and CS-7.…”

Section: Distribution Of Label In Phospholipidssupporting

confidence: 86%

“…Phospholipase A activity was previously demonstrated in N. gonorrhoeae strain 2686 by incubating cell envelope preparations with exogenous radioactively labeled phospholipids (3). The present study investigates the hydroly-L1PIDS, VOL.…”

Section: Phospholipid Hydrolysis In Cells Suspended In Buffermentioning

confidence: 84%

“…The release of these products suggests that phosphatidylethanolamine (PE), a major cell envelope component of Neisseria gonorrhoeae, is hydrolysed by phospholipase(s) (1). Further evidence for hydrolysis of PE in gonococci has been shown by the cellular accumulation of LPE in stationary phase cultures (2), and in cells which were suspended in buffer and lyophilized (3). In N.…”

Section: Introductionmentioning

confidence: 99%

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Phospholipid metabolism inNeisseria gonorrhoeae: Phospholipid hydrolysis in nongrowing cells

Cacciapuoti

Wegener

Morse

1979

Lipids

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Hydrolysis of cell envelope phospholipids was demonstrated in cells of both autolytic and nonautolytic strains of Neisseria gonorrhoeae that were labeled during growth in the presence of [3H] acetate. The label incorporated into the cellular phospholipids was located exclusively in the fatty acid acyl side chains. Labeled cells were incubated for 2 hr in N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid buffer, pH 8.5, containing various additions, and then examined for distribution of 3H in lipids. Ca++ selectively stimulated the deacylation of phosphatidylethanolamine (PE), whereas Mn++ stimulated the deacylation of phosphatidylglycerol (PG). Hydrolysis of phosphatidylethanolamine by phospholipase A was accompanied by the accumulation of lysophosphatidylethanolamine (LPE) and free fatty acids in the cells. Free fatty acids accumulated to a greater extent than lysophosphatidylethanolamine, suggesting that the latter was further hydrolyzed to glycerophosphorylethanolamine (GPE) and free fatty acids by a lysophospholipase. Methanol, ethanol, propanol, and isopropanol, added at concentrations which inhibited growth by 50%, stimulated phospholipase A, but not lysophospholipase activity. Differences in heat inactivation, metal ion requirements, and pH optima suggested that phospholipase A activities with phosphatidylethanolamine or phosphatidylglycerol as substrate and lysophospholipase may be separate enzymes.

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Section: Distribution Of Label In Phospholipidssupporting

confidence: 86%

Section: Phospholipid Hydrolysis In Cells Suspended In Buffermentioning

confidence: 84%

Section: Introductionmentioning

confidence: 99%

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Phospholipid metabolism inNeisseria gonorrhoeae: Phospholipid hydrolysis in nongrowing cells

Cacciapuoti

Wegener

Morse

1979

Lipids

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“…The presence of alternative enzymatic pathways for glycerophospholipid synthesis in Neisseria is supported by our analysis of the glycerophospholipid profile and acyltransferase activity of the nlaA mutants. Previous studies (Sud and Feingold, 1975;Senff et aL, 1976;Beebe and Wlodkowski, 1976;Cacciapuoti et aL 1979;Wolf-Watz et aL, 1975) have shown that PE comprises 70-80% and PG 15-20% of the total membrane phospholipids in N. gonorrhoeae. Insertional inactivation of the nlaA genes in both meningococci and gonococci decreased the PE and PG content with a concomitant increase in the precursor LPA and in other, unidentified phospholipids.…”

Section: Discussionmentioning

confidence: 92%

Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase

Swartley

Balthazar

Coleman

et al. 1995

Molecular Microbiology

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Lysophosphatidic acid (LPA) acyltransferases of Neisseria meningitidis and Neisseria gonorrhoeae were identified which share homology with other prokaryotic and eukaryotic LPA acyltransferases. In Escherichia coli, the conversion of LPA to phosphatidic acid, performed by the 1-acyl-sn-glycerol-3-phosphate acyltransferase PlsC, is a critical intermediate step in the biosynthesis of membrane glycerophospholipids. A Tn916-generated mutant of a serogroup B meningococcal strain was identified that exhibited increased amounts of capsular polysaccharide, as shown by colony immunoblots, and a threefold increase in the number of assembled pili. The single, truncated 3.8 kb Tn916 insertion in the meningococcal mutant was localized within a 771 bp open reading frame, The gonococcal equivalent of this gene was identified by transformation with the cloned meningococcal mutant gene. In N. gonorrhoeae, the mutation increased piliation fivefold. The insertions were found to be within a gene that was subsequently designated nlaA (neisserial LPA acyltransferase). The predicted neisserial LPA acyltransferases were homologous (>20% identity, >40% amino acid similarity) to the family of PlsC protein homologues. A cloned copy of the meningococcal nlaA gene complemented in trans a temperature-sensitive E. coli PlsCts- mutant. Tn916 and omega-cassette insertional inactivations of the neisserial nlaA genes altered the membrane glycerophospholipid compositions of both N. meningitidis and N. gonorrhoeae but were not lethal. Therefore, the pathogenic Neisseria spp. appear to be able to utilize alternative enzyme(s) to produce phosphatidic acid. This hypothesis is supported by the observation that, although the amounts of mature glycerophospholipids were altered in the meningococcal and the gonococcal nlaA mutants, glycerophospholipid synthesis was detectable at significant levels. In addition, acyltransferase enzymatic activity, while reduced in the gonococcal nlaA mutant, was increased in the meningococcal nlaA mutant. We postulate that the pathogenic Neisseria spp. are able to utilize alternate acyltransferases to produce glycerophospholipids in the absence of nlaA enzymatic activity. Implementation of these secondary enzymes results in alterations of glycerophospholipid composition that lead to pleiotropic effects on the cell surface components, including effects on capsule and piliation.

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“…Purity of the outer membrane was determined by measuring lactate dehydrogenase (EC 1.1.1.28) activity by the method of MacGregor and Schnaitman (29) and phospholipase A (EC 3.1.1.4) activity as described by Senff et al (49). The substrate for the phospholipase assay was [3H]PE prepared from Escherichia coli strain CA85 grown in GC base broth to which was added [2-3H]glycerol (0.625 ttCi/ml).…”

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confidence: 99%

Cell envelope alterations in antibiotic-sensitive and-resistant strains of Neisseria gonorrhoeae

Guymon¹,

Walstad²,

Sparling³

1978

J Bacteriol

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The cell envelopes of antibiotic-resistant and -sensitive isogenic strains of Neisseria gonorrhoeae were analyzed to determine whether acquisition of genetic loci for altered antibiotic sensitivity was accompanied by alterations in cell envelope composition. No differences in the composition of phospholipids and lipopolysaccharides were noted. Acquisition of mtr-2, which results in low-level, nonspecific increased resistance to multiple antibiotics, dyes, and detergents, was accompanied by a sevenfold increase in the amount of a minor, 52,000-molecularweight outer membrane protein and a 32% increase in the extent of peptidoglycan cross-linking. Subsequent addition of the nonspecific hypersensitivity loci env-1 or env-2 to a strain carrying mtr-2 resulted in reversal of the phenotypic resistance determined by mtr-2 and marked reduction in both the amount of the 52,000molecular-weight outer membrane protein and the extent of peptidoglycan crosslinking. Introduction of penB2, which results in a fourfold increase in resistance to penicillin and tetracycline, was accompanied by the disappearance of the principal outer membrane protein of the wild-type strain (molecular weight, 36,900) and the appearance of a new species of the principal outer membrane protein (molecular weight, 39,400) in the transformant. MATERIALS AND METHODSStrains used. The strains used in these studies 391 on July 16, 2020 by guest

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Phospholipid composition and phospholipase A activity of Neisseria gonorrhoeae

Cited by 42 publications

References 34 publications

Phospholipid metabolism inNeisseria gonorrhoeae: Phospholipid hydrolysis in nongrowing cells

Phospholipid metabolism inNeisseria gonorrhoeae: Phospholipid hydrolysis in nongrowing cells

Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase

Cell envelope alterations in antibiotic-sensitive and-resistant strains of Neisseria gonorrhoeae

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