Article Abstract:
Analysis of the outer membrane proteins of primary and secondary forms of Xenorhabdus nematophilus reveals OpnP as the most highly expressed outer membrane protein. Sequence analysis helps compare the amino acid composition of OpnP with those of the porin proteins OmpF and OmpC of Escherichia coli. During stationary-phase growth X. nematophilus produces three additional proteins, OpnA, OpnB, and OpnS. Growth temperature exerts no influence on the production of OpnS, while increase in temperature from 19 to 34 degrees Celsius significantly stimulates the production of OpnT. Secondary-form cells do not produce OpnA and OpnB.
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Article Abstract:
The envZ gene of Xenorhabdus nematophilus was inactivated to determine the role of the EnvZ histidine kinase sensor protein in the regulation of outer membrane protein (Opns) synthesis in the gram-negative bacterium. The envZ-null strain of Xenorhabdus nematophilus exhibited impaired Opn production and reduced the levels of OmpF-like pore-forming proteins. Furthermore, the envZ-null strain also exhibited reduced OpnS, OpnX and OpnB synthesis indicating the role of EnvZ histidine kinase sensor protein in the high-level production of Opns in bacterial cells during exponential growth.
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Article Abstract:
Xenorhabdus nematophilus lysogenic strain F1 produces the bacteriocide xenorhabdicin and phage head particles. Xenorhabdicin resembles the phage tail and contains two main subunits of 43 and 20 kDa which are the sheath and inner core and five smaller subunits. The phage particle has one main and two smaller subunits. Xenorhabdus nematophilus has a symbiotic relationship with pathogenic nematodes and xenorhabdicin prevents other closely related bacterial species from inhabiting the same nematode larvae.
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