In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in Pathogenesis
Leptospirosis is a zoonosis caused by the pathogenic bacteria of the genus <i>Leptospira</i>. The identification of conserved outer membrane proteins among pathogenic strains is a major research target in elucidating mechanisms of pathogenicity. Surface-exposed proteins are most probably...
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MDPI AG
2020-11-01
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| Series: | Tropical Medicine and Infectious Disease |
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| author | Brenda Bevilaqua Daroz Luis Guilherme Virgílio Fernandes Aline Florencio Teixeira Ana Lucia Tabet Oller Nascimento |
| author_facet | Brenda Bevilaqua Daroz Luis Guilherme Virgílio Fernandes Aline Florencio Teixeira Ana Lucia Tabet Oller Nascimento |
| author_sort | Brenda Bevilaqua Daroz |
| collection | DOAJ |
| description | Leptospirosis is a zoonosis caused by the pathogenic bacteria of the genus <i>Leptospira</i>. The identification of conserved outer membrane proteins among pathogenic strains is a major research target in elucidating mechanisms of pathogenicity. Surface-exposed proteins are most probably the ones involved in the interaction of leptospires with the environment. Some spirochetes use outer membrane proteases as a way to penetrate host tissues. HtrA is a family of proteins found in various cell types, from prokaryotes to primates. They are a set of proteases usually composed of a serine protease and PDZ domains, and they are generally transported to the periplasm. Here, we identified four genes—annotated as HtrA, LIC11111, LIC20143, LIC20144 and LIC11037—and another one annotated as a serine protease, LIC11112. It is believed that the last forms a functional heterodimer with LIC11111, since they are organized in one operon. Our analyses showed that these proteins are highly conserved among pathogenic strains. LIC11112, LIC20143, and LIC11037 have the serine protease domain with the conserved catalytic triad His-Asp-Ser. This is the first bioinformatics analysis of HtrA proteins from <i>Leptospira</i> that suggests their proteolytic activity potential. Experimental studies are warranted to elucidate this possibility. |
| first_indexed | 2024-03-10T14:29:36Z |
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| institution | Directory Open Access Journal |
| issn | 2414-6366 |
| language | English |
| last_indexed | 2024-03-10T14:29:36Z |
| publishDate | 2020-11-01 |
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| record_format | Article |
| series | Tropical Medicine and Infectious Disease |
| spelling | doaj.art-e40ea2309cca4d19b53dbd83dfd3c9772023-11-20T22:43:34ZengMDPI AGTropical Medicine and Infectious Disease2414-63662020-11-015417910.3390/tropicalmed5040179In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in PathogenesisBrenda Bevilaqua Daroz0Luis Guilherme Virgílio Fernandes1Aline Florencio Teixeira2Ana Lucia Tabet Oller Nascimento3Laboratório Especial de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-000, BrazilLaboratório Especial de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-000, BrazilLaboratório Especial de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-000, BrazilLaboratório Especial de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-000, BrazilLeptospirosis is a zoonosis caused by the pathogenic bacteria of the genus <i>Leptospira</i>. The identification of conserved outer membrane proteins among pathogenic strains is a major research target in elucidating mechanisms of pathogenicity. Surface-exposed proteins are most probably the ones involved in the interaction of leptospires with the environment. Some spirochetes use outer membrane proteases as a way to penetrate host tissues. HtrA is a family of proteins found in various cell types, from prokaryotes to primates. They are a set of proteases usually composed of a serine protease and PDZ domains, and they are generally transported to the periplasm. Here, we identified four genes—annotated as HtrA, LIC11111, LIC20143, LIC20144 and LIC11037—and another one annotated as a serine protease, LIC11112. It is believed that the last forms a functional heterodimer with LIC11111, since they are organized in one operon. Our analyses showed that these proteins are highly conserved among pathogenic strains. LIC11112, LIC20143, and LIC11037 have the serine protease domain with the conserved catalytic triad His-Asp-Ser. This is the first bioinformatics analysis of HtrA proteins from <i>Leptospira</i> that suggests their proteolytic activity potential. Experimental studies are warranted to elucidate this possibility.https://www.mdpi.com/2414-6366/5/4/179<i>Leptospira</i>leptospirosisHtrA proteinpathogenesis |
| spellingShingle | Brenda Bevilaqua Daroz Luis Guilherme Virgílio Fernandes Aline Florencio Teixeira Ana Lucia Tabet Oller Nascimento In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in Pathogenesis Tropical Medicine and Infectious Disease <i>Leptospira</i> leptospirosis HtrA protein pathogenesis |
| title | In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in Pathogenesis |
| title_full | In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in Pathogenesis |
| title_fullStr | In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in Pathogenesis |
| title_full_unstemmed | In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in Pathogenesis |
| title_short | In Silico Structural and Functional Characterization of HtrA Proteins of <i>Leptospira</i> spp.: Possible Implications in Pathogenesis |
| title_sort | in silico structural and functional characterization of htra proteins of i leptospira i spp possible implications in pathogenesis |
| topic | <i>Leptospira</i> leptospirosis HtrA protein pathogenesis |
| url | https://www.mdpi.com/2414-6366/5/4/179 |
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