The gonococcal NlpD protein facilitates cell separation by activating peptidoglycan cleavage by AmiC

Elizabeth A. Stohl, Jonathan D. Lenz, Joseph P. Dillard, H. Steven Seifert*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Key steps in bacterial cell division are the synthesis and subsequent hydrolysis of septal peptidoglycan (PG), which allow efficient separation of daughter cells. Extensive studies in the Gram-negative, rod-shaped bacterium Escherichia coli have revealed that this hydrolysis is highly regulated spatially and temporally. Neisseria gonorrhoeae is an obligate Gram-negative, diplococcal pathogen and is the only causative agent of the sexually transmitted infection gonorrhea. We investigated how cell separation proceeds in this diplococcal organism. We demonstrated that deletion of the nlpD gene in strain FA1090 leads to poor growth and to an altered colony and cell morphology. An isopropyl-beta-D-galactopyranoside (IPTG)-regulated nlpD complemented construct can restore these defects only when IPTG is supplied in the growth medium. Thin-section transmission electron microscopy (TEM) revealed that the nlpD mutant strain grew in large clumps containing live and dead bacteria, which was consistent with deficient cell separation. Biochemical analyses of purified NlpD protein showed that it was able to bind purified PG. Finally, we showed that, although NlpD has no hydrolase activity itself, NlpD potentiates the hydrolytic activity of AmiC. These results indicate that N. gonorrhoeae NlpD is required for proper cell growth and division through its interactions with the amidase AmiC.

Original languageEnglish (US)
Pages (from-to)615-622
Number of pages8
JournalJournal of bacteriology
Issue number4
StatePublished - 2016

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology


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