Molecular characterization of the pL40 protein inLeptospira interrogans

2009 ◽  
Vol 55 (6) ◽  
pp. 739-749
Author(s):  
Wei Zhao ◽  
Chun-Yan Chen ◽  
Xiang-Yan Zhang ◽  
Wei-Qiang Lai ◽  
Bao-Yu Hu ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Vaccine Candidate ◽  
Outer Membrane Proteins ◽  
Leptospira Interrogans ◽  
Major Focus ◽  
Pcr Screening ◽  
Low Passage ◽  
Mammalian Infection ◽  
Triton X

Leptospirosis is a widespread zoonotic disease caused by pathogenic leptospires. The identification of outer membrane proteins (OMPs) conserved among pathogenic leptospires, which are exposed on the leptospiral surface and expressed during mammalian infection, has become a major focus of leptospirosis research. pL40, a 40 kDa protein coded by the LA3744 gene in Leptospira interrogans , was found to be unique to Leptospira . Triton X-114 fractionation and flow cytometry analyses indicate that pL40 is a component of the leptospiral outer membrane. The conservation of pL40 among Leptospira strains prevalent in China was confirmed by both Western blotting and PCR screening. Furthermore, the pL40 antigen could be recognized by sera from guinea pigs and mice infected with low-passage L. interrogans. These findings indicate that pL40 may serve as a useful serodiagnostic antigen and vaccine candidate for L. interrogans.

scholarly journals Temperature-Regulated Protein Synthesis by Leptospira interrogans

2001 ◽  
Vol 69 (1) ◽  
pp. 400-404 ◽  
Author(s):  
Jarlath E. Nally ◽  
John F. Timoney ◽  
Brian Stevenson
Keyword(s):  
Protein Synthesis ◽  
Outer Membrane ◽  
Pathogenic Bacteria ◽  
Outer Membrane Proteins ◽  
Pathogen Transmission ◽  
Leptospira Interrogans ◽  
Outer Membrane Lipoprotein ◽  
Higher Temperature ◽  
Response To Temperature ◽  
Triton X

ABSTRACT Leptospira interrogans is an important mammalian pathogen. Transmission from an environmental source requires adaptations to a range of new environmental conditions in the organs and tissues of the infected host. Since many pathogenic bacteria utilize temperature to discern their environment and regulate the synthesis of appropriate proteins, we investigated the effects of temperature on protein synthesis in L. interrogans. Bacteria were grown for several days after culture temperatures were shifted from 30 to 37°C. Triton X-114 cellular fractionation identified several proteins of the cytoplasm, periplasm, and outer membrane for which synthesis was dependent on the culture temperature. Synthesis of a cytoplasmic protein of 20 kDa was switched off at 37°C, whereas synthesis of a 66-kDa periplasmic protein was increased at the higher temperature. Increased synthesis of a 25-kDa outer membrane protein was observed when the organisms were shifted from 30 to 37°C. A 36-kDa protein synthesized at 30 but not at 37°C was identified as LipL36, an outer membrane lipoprotein. In contrast, expression of another lipoprotein, LipL41, was the same at either temperature. Immunoblotting with convalescent equine sera revealed that some proteins exhibiting thermoregulation of synthesis elicited antibody responses during infection. Our results show that sera from horses which aborted as a result of naturally acquired infection withL. interrogans serovar pomona type kennewicki recognize periplasmic and outer membrane proteins which are differentially synthesized in response to temperature and which therefore may be important in the host-pathogen interaction during infection.

Triton X‐114 Fractionated Subcellular Proteome of Leptospira interrogans Shows Selective Enrichment of Pathogenic and Outer Membrane Proteins in the Detergent Fraction

PROTEOMICS ◽  
2020 ◽  
Vol 20 (19-20) ◽  
pp. 2000170
Author(s):  
Sikha Thoduvayil ◽  
Gunasekaran Dhandapani ◽  
Rahul Brahma ◽  
Rex Devasahayam Arokia Balaya ◽  
Kiran K. Mangalaparthi ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Leptospira Interrogans ◽  
Selective Enrichment ◽  
Triton X
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