A Trojan horse mechanism of bacterial pathogenesis against nematodes.
Understanding the mechanisms of host-pathogen interaction can provide crucial information for successfully manipulating their relationships. Because of its genetic background and practical advantages over vertebrate model systems, the nematode Caenorhabditis elegans model has become an attractive host for studying microbial pathogenesis. Here we report a "Trojan horse" mechanism of bacterial pathogenesis against nematodes. We show that the bacterium Bacillus nematocida B16 lures nematodes by emitting potent volatile organic compounds that are much more attractive to worms than those from ordinary dietary bacteria. Seventeen B. nematocida-attractant volatile organic compounds are identified, and seven are individually confirmed to lure nematodes. Once the bacteria enter the intestine of nematodes, they secrete two proteases with broad substrate ranges but preferentially target essential intestinal proteins, leading to nematode death. This Trojan horse pattern of bacterium-nematode interaction enriches our understanding of microbial pathogenesis.
Niu
Qiuhong
Q
Laboratory for Conservation and Utilization of Bio-Resources, Yunnan University, Kunming, Yunnan 650091, People's Republic of China.
Huang
Xiaowei
X
Zhang
Lin
L
Xu
Jianping
J
Yang
Dongmei
D
Wei
Kangbi
K
Niu
Xuemei
X
An
Zhiqiang
Z
Bennett
Joan Wennstrom
JW
Zou
Chenggang
C
Yang
Jinkui
J
Zhang
Ke-Qin
KQ
D000818:Animals; D001407:Bacillus / Q000472:pathogenicity* / Q000502:physiology; D017173:Caenorhabditis elegans / Q000382:microbiology* / Q000502:physiology; D054884:Host-Pathogen Interactions / Q000502:physiology*; D007422:Intestines / Q000382:microbiology; D009812:Odorants; D010447:Peptide Hydrolases / Q000378:metabolism; D012987:Soil / Q000469:parasitology; D014774:Virulence / Q000502:physiology; D037521:Virulence Factors / Q000378:metabolism; D055549:Volatile Organic Compounds / Q000378:metabolism
D012987:Soil; D037521:Virulence Factors; D055549:Volatile Organic Compounds; D010447:Peptide Hydrolases