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The Neisseria gonorrhoeae lpxLII gene encodes for a late-functioning lauroyl acyl transferase, and a null mutation within the gene has a significant effect on the induction of acute inflammatory responses

Lookup NU author(s): Charles Ellis, Dr Anjam Khan, Dr Raquel Demarco De Hormaeche

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Abstract

LPS is a fundamental constituent of the outer membrane of all Gram-negative bacteria, and the lipid A domain plays a central role in the induction of inflammatory responses. We identified genes of the Neisseria gonorrhoeae lipid A biosynthetic pathway by searching the complete gonococcal genome sequence with sequences of known enzymes from other species. The lpxLII gene was disrupted by an insertion-deletion in an attenuated aroA mutant of the gonococcal strain MS11. Lipopolysaccharide (LPS) and lipid A analysis demonstrated that the lpxLII mutant had synthesized an altered LPS molecule lacking a single lauric fatty acid residue in the GlcN II of the lipid A backbone. LPS of the lpxLII mutant had a markedly reduced ability to induce the proinflammatory cytokines tumour necrosis factor (TNF)-α, interleukin (IL)-1β, IL-6 and IL-8 from human macrophages and IL-8 from polymorphonuclear cells. This study demonstrates that the lpxLII gene in gonococci encodes for a late-functioning lauroyl acyl transferase that adds a lauric acid at position 2′ in the lipid A backbone. The presence of lauric acid at such a position appears to be crucial for the induction of full inflammatory responses by N. gonorrhoeae LPS.


Publication metadata

Author(s): Ellis CD, Lindner B, Khan CMA, Zahringer U, Demarco De Hormaeche R

Publication type: Article

Publication status: Published

Journal: Molecular Microbiology

Year: 2001

Volume: 42

Issue: 1

Pages: 167-181

ISSN (print): 0950-382X

ISSN (electronic): 1365-2958

Publisher: Wiley-Blackwell

URL: http://dx.doi.org/10.1046/j.1365-2958.2001.02619.x

DOI: 10.1046/j.1365-2958.2001.02619.x

PubMed id: 11679076


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