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  1. Article ; Online: Extracellular Proteome Analysis Shows the Abundance of Histidine Kinase Sensor Protein, DNA Helicase, Putative Lipoprotein Containing Peptidase M75 Domain and Peptidase C39 Domain Protein in Leptospira interrogans Grown in EMJH Medium

    Abhijit Sarma / Dhandapani Gunasekaran / Devasahayam Arokia Balaya Rex / Thoduvayil Sikha / Homen Phukan / Kumar Mangalaparthi Kiran / Sneha M. Pinto / Thottethodi Subrahmanya Keshava Prasad / Madathiparambil G. Madanan

    Pathogens, Vol 10, Iss 852, p

    2021  Volume 852

    Abstract: Leptospirosis is a re-emerging form of zoonosis that is caused by the spirochete pathogen Leptospira . Extracellular proteins play critical roles in the pathogenicity and survival of this pathogen in the host and environment. Extraction and analysis of ... ...

    Abstract Leptospirosis is a re-emerging form of zoonosis that is caused by the spirochete pathogen Leptospira . Extracellular proteins play critical roles in the pathogenicity and survival of this pathogen in the host and environment. Extraction and analysis of extracellular proteins is a difficult task due to the abundance of enrichments like serum and bovine serum albumin in the culture medium, as is distinguishing them from the cellular proteins that may reach the analyte during extraction. In this study, extracellular proteins were separated as secretory proteins from the culture supernatant and surface proteins were separated during the washing of the cell pellet. The proteins identified were sorted based on the proportion of the cellular fractions and the extracellular fractions. The results showed the identification of 56 extracellular proteins, out of which 19 were exclusively extracellular. For those proteins, the difference in quantity with respect to their presence within the cell was found to be up to 1770-fold. Further, bioinformatics analysis elucidated characteristics and functions of the identified proteins. Orthologs of extracellular proteins in various Leptospira species were found to be closely related among different pathogenic forms. In addition to the identification of extracellular proteins, this study put forward a method for the extraction and identification of extracellular proteins.
    Keywords Leptospira ; protein ; extracellular ; surface ; secretory ; pathogenic ; Medicine ; R
    Subject code 500 ; 580
    Language English
    Publishing date 2021-07-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article: Heterologous Expression, Purification and Characterization of an Oligopeptidase A from the Pathogen Leptospira interrogans

    Anu, PrasannanV / Madathiparambil G. Madanan / Ananthakrishnan J. Nair / Gangaprasad A. Nair / Govinda Pillai M. Nair / Perumana R. Sudhakaran / Padikara K. Satheeshkumar

    Molecular biotechnology. 2018 Apr., v. 60, no. 4

    2018  

    Abstract: Oligopeptidases are enzymes involved in the degradation of short peptides (generally less than 30 amino acids in size) which help pathogens evade the host defence mechanisms. Leptospira is a zoonotic pathogen and causes leptospirosis in mammals. Proteome ...

    Abstract Oligopeptidases are enzymes involved in the degradation of short peptides (generally less than 30 amino acids in size) which help pathogens evade the host defence mechanisms. Leptospira is a zoonotic pathogen and causes leptospirosis in mammals. Proteome analysis of Leptospira revealed the presence of oligopeptidase A (OpdA) among other membrane proteins. To study the role of oligopeptidase in leptospirosis, the OpdA of L. interrogans was cloned and expressed in Escherichia coli with a histidine tag (His-tag). The protein showed maximum expression at 37 °C with 0.5 mM of IPTG after 2 h of induction. Recombinant OpdA protein was purified to homogeneity using Ni-affinity chromatography. The purified OpdA showed more than 80% inhibition with a serine protease inhibitor but the activity was reduced to 30% with the cysteine protease inhibitor. The peptidase activity was increased significantly in the presence of Zn²⁺ at a neutral pH. Inhibitor assay indicate the presence of more than one active sites for peptidase activity as reported with the OpdA of E. coli and Salmonella. Over-expression of OpdA in E. coli BL21 (DE3) did not cause any negative effects on normal cell growth and viability. The role of OpdA as virulence factor in Leptospira and its potential as a therapeutic and diagnostic target in leptospirosis is yet to be identified.
    Keywords Escherichia coli ; Leptospira interrogans ; Salmonella ; active sites ; cell growth ; chromatography ; cysteine proteinase inhibitors ; defense mechanisms ; enzyme activity ; heterologous gene expression ; histidine ; leptospirosis ; mammals ; membrane proteins ; pH ; pathogens ; peptides ; proteome ; serine proteinases ; viability ; virulence ; zinc
    Language English
    Dates of publication 2018-04
    Size p. 302-309.
    Publishing place Springer US
    Document type Article
    ZDB-ID 1193057-3
    ISSN 1559-0305 ; 1073-6085
    ISSN (online) 1559-0305
    ISSN 1073-6085
    DOI 10.1007/s12033-018-0073-8
    Database NAL-Catalogue (AGRICOLA)

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