Mol Ecol 1999, 8:1683–1691 PubMedCrossRef 58 Matalon Y, Katzir N

Mol Ecol 1999, 8:1683–1691.PubMedCrossRef 58. Matalon Y, Katzir N, Gottlieb Y, Portnoy V, Zchori-Fein E: Cardinium in Plagiomerus diaspidis (Hymenoptera: Encyrtidae). J Invertebr Pathol 2007, 96:106–8.PubMedCrossRef Authors’ contributions MS performed the experiments. SK participated in rearing the whitefly populations and performing some of the experiments. MS, KZ, SGB and MG collected whitefly

populations in Croatia. MG and MS designed the study. MG drafted the manuscript. All authors have read and approved the final manuscript.”
“Background Photorhabdus bacteria are pathogens of insects, and obligate symbionts with insect-pathogenic Heterorhabditid nematodes [1, 2]. These host nematodes invade an insect and regurgitate the bacteria from see more their gut [3]. The bacteria then colonize the infected insect and release both insecticides that kill the insect host and antibiotics to kill any invading and competing microbes [4]. Following several rounds of nematode and this website bacterial replication, a new generation of infective juvenile (IJ) nematodes re-uptake the bacteria and exit

the cadaver to find new hosts [1]. This dual requirement for symbiosis and virulence makes Photorhabdus an excellent model organism for studying bacterial colonization and developmental behaviour in addition to a potential AZD1152 cost source of potent new insecticidal proteins and antibiotics [2]. The genus Photorhabdus comprises three distinct species: P. temperata, P. luminescens and P. asymbiotica. Although all three are highly pathogenic to insects, P. asymbiotica was originally isolated from human wounds and its nematode vector has only recently been identified [5]. Little is known about transmission into human patients, but P. asymbiotica is unique in the genus in being able to grow at 37°C and is considered an emerging human pathogen [6]. In an attempt to find potential host-interacting proteins that are relevant to either human or insect infections we used two-dimensional

(2D) gel electrophoresis to compare supernatant proteins secreted at 28°C and 37°C. We identified a number of proteins that were differentially produced at these temperatures. Two small proteins were of particular interest, because they were secreted at a very high level at 28°C but were not detectable at the clinically relevant Farnesyltransferase temperature of 37°C. One of these proteins was encoded by a gene on a plasmid found only in P. asymbiotica strains. The other was encoded by a chromosomal gene previously identified in a proteomic study of P. luminescens TT01 [7]. We present here the first detailed investigation into the role of this second highly secreted protein present in both P. luminescens and P. asymbiotica. Results Identification of Pam by two-dimensional electrophoretic analysis of the P. asymbiotica ATCC43949 secreted proteins Given the availability of P.

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