LuxR solos in Photorhabdus species

被引:30
作者
Brameyer, Sophie [1 ]
Kresovic, Darko [2 ]
Bode, Helge B. [2 ]
Heermann, Ralf [1 ]
机构
[1] Univ Munich, Bereich Mikrobiol, Biozentrum, Munich, Germany
[2] Goethe Univ Frankfurt, Fachbereich Biowissensch, D-60438 Frankfurt, Germany
关键词
LuxR solos; quorum sensing; cell-cell communication; quorum quenching; entomopathogenic bacteria; QUORUM-SENSING SIGNAL; HOMOSERINE LACTONE; SUBSP NOV; ASYMBIOTICA; SPECIFICITY; BACTERIA; ENZYME; IDENTIFICATION; PATHOGENICITY; COMMUNICATION;
D O I
10.3389/fcimb.2014.00166
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Bacteria communicate via small diffusible molecules to mediate group-coordinated behavior, a process designated as quorum sensing. The basic molecular quorum sensing system of Gram-negative bacteria consists of a Luxl-type autoinducer synthase producing acyl-homoserine lactones (AHLs) as signaling molecules, and a LuxR-type receptor detecting the AHLs to control expression of specific genes. However, many proteobacteria possess one or more unpaired LuxR-type receptors that lack a cognate Luxl-like synthase, referred to as LuxR solos. The enteric and insect pathogenic bacteria of the genus Photorhabdus harbor an extraordinarily high number of LuxR solos, more than any other known bacteria, and all lack a Luxl-like synthase. Here, we focus on the presence and the different types of LuxR solos in the three known Photorhabdus species using bioinformatics analyses. Generally, the N-terminal signal-binding domain (SBD) of LuxR-type receptors sensing AHLs have a motif of six conserved amino acids that is important for binding and specificity of the signaling molecule. However, this motif is altered in the majority of the Photorhabdus-specific LuxR solos, suggesting the use of other signaling molecules than AHLs. Furthermore, all Photorhabdus species contain at least one LuxR solo with an intact AHL-binding motif, which might allow the ability to sense AHLs of other bacteria. Moreover, all three species have high AHL-degrading activity caused by the presence of different AHL-lactonases and AHL-acylases, revealing a high quorum quenching activity against other bacteria. However, the majority of the other LuxR solos in Photorhabdus have a N-terminal so-called PAS4-domain instead of an AHL-binding domain, containing different amino acid motifs than the AHL-sensors, which potentially allows the recognition of a highly variable range of signaling molecules that can be sensed apart from AHLs. These PAS4-LuxR solos are proposed to be involved in host sensing, and therefore in inter-kingdom signaling. Overall, Photorhabdus species are perfect model organisms to study bacterial communication via LuxR solos and their role for a symbiotic and pathogenic life style.
引用
收藏
页数:11
相关论文
共 48 条
[1]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[2]   The PAS domain-containing histidine kinase RpfS is a second sensor for the diffusible signal factor of Xanthomonas campestris [J].
An, Shi-Qi ;
Allan, John H. ;
McCarthy, Yvonne ;
Febrer, Melanie ;
Dow, J. Maxwell ;
Ryan, Robert P. .
MOLECULAR MICROBIOLOGY, 2014, 92 (03) :586-597
[3]   Autoinducers Act as Biological Timers in Vibrio harveyi [J].
Anetzberger, Claudia ;
Reiger, Matthias ;
Fekete, Agnes ;
Schell, Ursula ;
Stambrau, Nina ;
Plener, Laure ;
Kopka, Joachim ;
Schmitt-Kopplin, Phillippe ;
Hilbi, Hubert ;
Jung, Kirsten .
PLOS ONE, 2012, 7 (10)
[4]   Cross-species induction of luminescence in the quorum-sensing bacterium Vibrio harveyi [J].
Bassler, BL ;
Greenberg, EP ;
Stevens, AM .
JOURNAL OF BACTERIOLOGY, 1997, 179 (12) :4043-4045
[5]   Production of acylated homoserine lactone by Gram-positive bacteria isolated from marine water [J].
Biswa, Pramal ;
Doble, Mukesh .
FEMS MICROBIOLOGY LETTERS, 2013, 343 (01) :34-41
[6]  
Brachmann AO, 2013, NAT CHEM BIOL, V9, P573, DOI [10.1038/NCHEMBIO.1295, 10.1038/nchembio.1295]
[7]   AHL-driven quorum-sensing circuits: their frequency and function among the Proteobacteria [J].
Case, Rebecca J. ;
Labbate, Maurizio ;
Kjelleberg, Staffan .
ISME JOURNAL, 2008, 2 (04) :345-349
[8]   Structural Basis of Acyl-homoserine Lactone-Dependent Signaling [J].
Churchill, Mair E. A. ;
Chen, Lingling .
CHEMICAL REVIEWS, 2011, 111 (01) :68-85
[9]   Photorhabdus: a model for the analysis of pathogenicity and mutualism [J].
Clarke, David J. .
CELLULAR MICROBIOLOGY, 2008, 10 (11) :2159-2167
[10]   Complete Genome Sequence of the Extreme Thermophile Dictyoglomus thermophilum H-6-12 [J].
Coil, David A. ;
Badger, Jonathan H. ;
Forberger, Heather C. ;
Riggs, Florenta ;
Madupu, Ramana ;
Fedorova, Nadia ;
Ward, Naomi ;
Robb, Frank T. ;
Eisen, Jonathan A. .
GENOME ANNOUNCEMENTS, 2014, 2 (01)