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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Characterization of a novel protein of Leptospira interrogans exhibiting plasminogen, vitronectin and complement binding properties

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Author(s):
Cavenague, Maria F. [1, 2] ; Teixeira, Aline F. [1] ; Filho, Antonio S. [3] ; Souza, Gisele O. [3] ; Vasconcellos, Silvio A. [3] ; Heinemann, Marcos B. [3] ; Nascimento, Ana L. T. O. [1, 2]
Total Authors: 7
Affiliation:
[1] Inst Butantan, Lab Especial Desenvolvimento Vacinas, Ctr Biotecnol, Ave Vital Brazil 1500, BR-05503900 Sao Paulo, SP - Brazil
[2] Univ Sao Paulo, Programa Posgrad Interunidades Biotecnol, Inst Ciencias Biomed, Sao Paulo, SP - Brazil
[3] Univ Sao Paulo, Lab Zoonoses Bacterianas, Fac Med Vet & Zootecnia, Sao Paulo, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY; v. 309, n. 2, p. 116-129, MAR 2019.
Web of Science Citations: 2
Abstract

Leptospirosis is a severe zoonosis caused by pathogenic species of the genus Leptospira. This work focuses on a hypothetical protein of unknown function, encoded by the gene LIC13259, and predicted to be a surface protein, widely distributed among pathogenic leptospiral strain. The gene was amplified from L. interrogans serovar Copenhageni, strain Fiocruz L1-130, cloned and the protein expressed using Escherichia coil as a host system. Immunofluorescence assay showed that the protein is surface-exposed. The recombinant protein LIC13259 (rLIC13259) has the ability to interact with the extracellular matrix (ECM) laminin, in a dose-dependent manner but saturation was not reach. The rLIC13259 protein is a plasminogen (PLG)-binding protein, generating plasmin, in the presence of urokinase PLG-activator uPA. The recombinant protein is able to mediate the binding to human purified terminal complement route vitronectin, C7, C8 and C9, and to recruit and interact with these components from normal human serum (NHS). These interactions are dose-dependent on NHS increased concentration. The binding of rLIC13259 to C8 and vitronectin was slight and pronounced inhibited in the presence of increasing heparin concentration, respectively, suggesting that the interaction with vitronectin occurs via heparin domain. Most interesting, the interaction of rLIC13259 with C9 protein was capable of preventing C9 polymerization, suggesting that the membrane attack complex (MAC) formation was inhibited. Thus, we tentatively assign the coding sequence (CDS) LIC13259, previously annotated as unknown function, as a novel protein that may play an important role in the host's invasion and immune evasion processes, contributing to the establishment of the leptospiral infection. (AU)

FAPESP's process: 16/04295-3 - Interaction of two Leptospira interrogans proteins to plasma and extracellular matrix components of the host.
Grantee:Maria Fernanda Cavenague Pereira
Support type: Scholarships in Brazil - Master
FAPESP's process: 14/50981-0 - Search for surface proteins among the genome sequences of Leptospira interrogans: functional and immunological characterization to understanding mechanisms involved in the bacterial pathogenesis
Grantee:Ana Lucia Tabet Oller Do Nascimento
Support type: Research Projects - Thematic Grants
FAPESP's process: 16/11541-0 - "Evaluation of immunoprotective potential of CD4+ T-cell epitopes identified in proteins of Leptospira interrogans"
Grantee:Aline Rodrigues Florêncio Teixeira
Support type: Scholarships in Brazil - Post-Doctorate