A dual role of extracellular DNA during biofilm formation of Neisseria meningitidis.
Major pathogenic clonal complexes (cc) of Neisseria meningitidis differ substantially in their point prevalence among healthy carriers. We show that frequently carried pathogenic cc (e.g. sequence type ST-41/44 cc and ST-32 cc) depend on extracellular DNA (eDNA) to initiate in vitro biofilm formation, whereas biofilm formation of cc with low point prevalence (ST-8 cc and ST-11 cc) was eDNA-independent. For initial biofilm formation, a ST-32 cc type strain, but not a ST-11 type strain, utilized eDNA. The release of eDNA was mediated by lytic transglycosylase and cytoplasmic N-acetylmuramyl-L-alanine amidase genes. In late biofilms, outer membrane phospholipase A-dependent autolysis, which was observed in most cc, but not in ST-8 and ST-11 strains, was required for shear force resistance of microcolonies. Taken together, N. meningitidis evolved two different biofilm formation strategies, an eDNA-dependent one yielding shear force resistant microcolonies, and an eDNA-independent one. Based on the experimental findings and previous epidemiological observations, we hypothesize that most meningococcal cc display a settler phenotype, which is eDNA-dependent and results in a stable interaction with the host. On the contrary, spreaders (ST-11 and ST-8 cc) are unable to use eDNA for biofilm formation and might compensate for poor colonization properties by high transmission rates.
Lappann
Martin
M
University of Würzburg, Institute for Hygiene and Microbiology, Germany. mlappann@hygiene.uni-wuerzburg.de
Claus
Heike
H
van Alen
Tessa
T
Harmsen
Morten
M
Elias
Johannes
J
Molin
Søren
S
Vogel
Ulrich
U
D001426:Bacterial Proteins / Q000378:metabolism; D001433:Bacteriolysis; D018441:Biofilms / Q000254:growth & development*; D004269:DNA, Bacterial / Q000378:metabolism*; D016695:Glycosyltransferases / Q000378:metabolism; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism; D009345:Neisseria meningitidis / Q000166:cytology / Q000254:growth & development / Q000378:metabolism / Q000502:physiology*; D010740:Phospholipases / Q000378:metabolism
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D016695:Glycosyltransferases; D010740:Phospholipases; D009238:N-Acetylmuramoyl-L-alanine Amidase