Outer membrane proteins of three pathogenic Leptospira species

1993 ◽  
Vol 36 (1-2) ◽  
pp. 123-138 ◽  
Author(s):  
Vivian M. Nicholson ◽  
John F. Prescott
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Pathogenic Leptospira ◽  
Leptospira Species

scholarly journals Correction: Fine Mapping of the Interaction between C4b-Binding Protein and Outer Membrane Proteins LigA and LigB of Pathogenic Leptospira interrogans

2015 ◽  
Vol 9 (12) ◽  
pp. e0004286 ◽  
Author(s):  
Leandro C. D. Breda ◽  
Ching-Lin Hsieh ◽  
Mónica M. Castiblanco Valencia ◽  
Ludmila B. da Silva ◽  
Angela S. Barbosa ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Fine Mapping ◽  
Binding Protein ◽  
Outer Membrane Proteins ◽  
Leptospira Interrogans ◽  
Pathogenic Leptospira

scholarly journals Fine Mapping of the Interaction between C4b-Binding Protein and Outer Membrane Proteins LigA and LigB of Pathogenic Leptospira interrogans

2015 ◽  
Vol 9 (10) ◽  
pp. e0004192 ◽  
Author(s):  
Leandro C. D. Breda ◽  
Ching-Lin Hsieh ◽  
Mónica M. Castiblanco Valencia ◽  
Ludmila B. da Silva ◽  
Angela S. Barbosa ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Fine Mapping ◽  
Binding Protein ◽  
Outer Membrane Proteins ◽  
Leptospira Interrogans ◽  
Pathogenic Leptospira

scholarly journals Simultaneous detection of LipL32 and LipL21 genes of pathogenic leptospira from serum samples of bovines by multiplex PCR

2011 ◽  
Vol 1 (1) ◽  
pp. 15
Author(s):  
Timiri V. Meenambigai ◽  
Gopalakrishnan Ravikumar ◽  
Andy Srithar ◽  
Govindan Balakrishnan ◽  
Chidambaram Saranya ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Multiplex Pcr ◽  
Outer Membrane ◽  
Vaccine Development ◽  
Outer Membrane Proteins ◽  
Simultaneous Detection ◽  
Serum Samples ◽  
Pathogenic Leptospira ◽  
Annealing Conditions ◽  
Reference Strains

<p>Leptospirosis is a worldwide zoonotic disease of cattle associated with pathogenic leptospiral infection. This study focuses in the use of a molecular tool to detect pathogenic leptospiral infection in bovines by targeting the outer membrane proteins LipL32 and LipL21 simultaneously in a multiplex PCR. Sixteen pathogenic reference strains and 10 bovine serum samples were analyzed for simultaneous detection of both genes at appropriate annealing conditions. These findings are suggestive of the fact that multiplex PCR can be used to detect major outer membrane proteins of pathogenic leptospira from serum samples. Further it aided in the differentiation of pathogenic and non-pathogenic species of leptospires too. This study will definitely serve as a valuable tool, as it suggests the importance of <em>LipL32</em> genes as potential candidates for vaccine development to control animal Leptospirosis.</p>

scholarly journals Genetic manipulation of pathogenic Leptospira: CRISPR interference (CRISPRi)-mediated gene silencing and rapid mutant recovery at 37 °C

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
L. G. V. Fernandes ◽  
R. L. Hornsby ◽  
A. L. T. O. Nascimento ◽  
J. E. Nally
Keyword(s):  
Membrane Proteins ◽  
Gene Silencing ◽  
Outer Membrane ◽  
Genetic Manipulation ◽  
Outer Membrane Proteins ◽  
Pathogenic Leptospira ◽  
Pathogenic Mechanisms ◽  
Crispr Interference ◽  
Novel Studies ◽  
Genes Encoding

AbstractLeptospirosis is a neglected, widespread zoonosis caused by pathogenic species of the genus Leptospira, and is responsible for 60,000 deaths per year. Pathogenic mechanisms of leptospirosis remain poorly understood mainly because targeted mutations or gene silencing in pathogenic Leptospira continues to be inherently inefficient, laborious, costly and difficult to implement. In addition, pathogenic leptospires are highly fastidious and the selection of mutants on solid agar media can take up to 6 weeks. The catalytically inactive Cas9 (dCas9) is an RNA-guided DNA-binding protein from the Streptococcus pyogenes CRISPR/Cas system and can be used for gene silencing, in a strategy termed CRISPR interference (CRISPRi). Here, this technique was employed to silence genes encoding major outer membrane proteins of pathogenic L. interrogans. Conjugation protocols were optimized using the newly described HAN media modified for rapid mutant recovery at 37 °C in 3% CO2 within 8 days. Complete silencing of LipL32 and concomitant and complete silencing of both LigA and LigB outer membrane proteins were achieved, revealing for the first time that Lig proteins are involved in pathogenic Leptospira serum resistance. Gene silencing in pathogenic leptospires and rapid mutant recovery will facilitate novel studies to further evaluate and understand pathogenic mechanisms of leptospirosis.

scholarly journals Comparative Proteomics Study of Outer Membrane Proteins from three Pathogenic Leptospira Species used in Vaccine

2015 ◽  
Vol 5 (3) ◽  
pp. 753-760
Author(s):  
Khosrow Aghaiypour Kolyani ◽  
Rahman Shokri
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Double Diffusion ◽  
Pathogenic Leptospira ◽  
Sds Page ◽  
Antigenic Properties ◽  
Molecular Masses

 Background and Objective: Outer Membrane Proteins (OMPs) have an important role in pathogenecity and immunogenecity of Leptospira introgans. The aim of this study was chemical and immunological analysis of OMP extracted from three vaccinal strains of pathogenic Leptospira (L. canicola, L. grippotyphosa & L. sejroae hardjo) by electrophoresis and western blotting.Materials and Methods: Outer membrane enriched fractions that are insoluble in sodium N- lauryl sarcosinate isolated and studied by Sodium dodecyl sulfate – polyacrylamide gel electrophoresis. For identifying of antigenic properties of different proteins in three strains, antiserums developed in rabbit against the whole three valent vaccine and also  specific OMPs rom each of three Leptospira strains. The antiserum was used for immunological studies with immuno double diffusion and western blotting.Results: in SDS-PAGE five common protein bands with approximate molecular masses of 75,36,25,23 and 19 KDa were identified. After western blot studies identified four or five immunogenic band. In general, antiserum against L. grippotyphosa OMP has the highest ability in detecting common bands between three strains.Conclusion: Chemical and immunological comparisons between OMPs of the three strains which are being used in the commercial vaccine, provided useful documents to assess and maybe improve vaccine quality.  It indicated that OMPs are one of the major Leptospira component contributing in immunity and protectivity. Comparison between individual OMPs of each serotype revealed that L. grippotyphosa ones could contribute more in vaccine induced protectively in comparison with the other two serotypes.

scholarly journals The Conservation of Low Complexity Regions in Bacterial Proteins Depends on the Pathogenicity of the Strain and Subcellular Location of the Protein

Genes ◽  
2021 ◽  
Vol 12 (3) ◽  
pp. 451
Author(s):  
Pablo Mier ◽  
Miguel A. Andrade-Navarro
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Bacterial Species ◽  
Outer Membrane Proteins ◽  
Subcellular Location ◽  
Low Complexity ◽  
Extracellular Proteins ◽  
Bacterial Strains ◽  
Bacterial Proteins ◽  
Protein Subcellular Location

Low complexity regions (LCRs) in proteins are characterized by amino acid frequencies that differ from the average. These regions evolve faster and tend to be less conserved between homologs than globular domains. They are not common in bacteria, as compared to their prevalence in eukaryotes. Studying their conservation could help provide hypotheses about their function. To obtain the appropriate evolutionary focus for this rapidly evolving feature, here we study the conservation of LCRs in bacterial strains and compare their high variability to the closeness of the strains. For this, we selected 20 taxonomically diverse bacterial species and obtained the completely sequenced proteomes of two strains per species. We calculated all orthologous pairs for each of the 20 strain pairs. Per orthologous pair, we computed the conservation of two types of LCRs: compositionally biased regions (CBRs) and homorepeats (polyX). Our results show that, in bacteria, Q-rich CBRs are the most conserved, while A-rich CBRs and polyA are the most variable. LCRs have generally higher conservation when comparing pathogenic strains. However, this result depends on protein subcellular location: LCRs accumulate in extracellular and outer membrane proteins, with conservation increased in the extracellular proteins of pathogens, and decreased for polyX in the outer membrane proteins of pathogens. We conclude that these dependencies support the functional importance of LCRs in host–pathogen interactions.

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