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Literature summary for 2.7.8.43 extracted from

  • Handing, J.W.; Criss, A.K.
    The lipooligosaccharide-modifying enzyme LptA enhances gonococcal defence against human neutrophils (2015), Cell. Microbiol., 17, 910-921.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.8.43

Cloned(Commentary)

Cloned (Comment) Organism
gene lptA Neisseria gonorrhoeae

Protein Variants

Protein Variants Comment Organism
additional information construction of gene lptA mutant and complement strains from strain FA 1090 Neisseria gonorrhoeae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diacylphosphatidylethanolamine + lipid A Neisseria gonorrhoeae addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
 ?
diacylphosphatidylethanolamine + lipid A Neisseria gonorrhoeae FA 1090 addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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 ?

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae Q5F6F3 gene lptA
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Neisseria gonorrhoeae FA 1090 Q5F6F3 gene lptA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria gonorrhoeae diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
 ?
diacylphosphatidylethanolamine + lipid A addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A Neisseria gonorrhoeae FA 1090 diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
 ?

Synonyms

Synonyms Comment Organism
lipooligosaccharide phosphoethanolamine transferase A
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 Neisseria gonorrhoeae
LOS PEA transferase A
-
 Neisseria gonorrhoeae
LptA
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 Neisseria gonorrhoeae

General Information

General Information Comment Organism
malfunction loss of the enzyme activity increases bacterial sensitivity to killing by human complement and cationic antimicrobial peptides, lptA mutant Neisseria gonorrhoeae is significantly more sensitive to killing by human neutrophils Neisseria gonorrhoeae
physiological function LptA is important for Neisseria gonorrhoeae defence against non-oxidative components produced by polymorphonuclear leukocytes, PMNs. Infection of humans with Neisseria gonorrhoeae is marked by an influx of neutrophils to the site of infection. Enzyme LptA-catalysed modification of lipooligosaccharide enhances gonococcal defence against human neutrophils and enhances survival of the bacteria from the human inflammatory response during acute gonorrhoea. Three mechanisms underlie the increased sensitivity of lptA mutant bacteria to neutrophils: (i) lptA mutant bacteria are more likely to reside in mature phagolysosomes than LptA expressing bacteria, (ii) lptA mutant bacteria are more sensitive to killing by components found in neutrophil granules, including CAP37/azurocidin, human neutrophil peptide 1 and the serine protease cathepsin G, (iii) lptA mutant bacteria are more susceptible to killing by antimicrobial components that are exocytosed from neutrophils, including those decorating neutrophil extracellular traps Neisseria gonorrhoeae