Modeling the Trypanosoma cruzi Tc85-11 protein and mapping the laminin-binding site

Marroquin-Quelopana, Miryam; Oyama, Sílvia Maria Ribeiro; Pertinhez, Thelma A.; Spisni, Alberto; Juliano, María A.; Juliano, Luiz; Colli, Walter; Alves, Maria Júlia M.

doi:10.1016/j.bbrc.2004.10.068

Cited by 27 publications

(28 citation statements)

References 33 publications

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“…The structure of Tc85-11, a family member with laminin-binding property implicated in host cell invasion, has been determined (Giordano et al 1999 ;Marroquin-Quelopana et al 2004 ). As compared to MT gp82 sequence, Tc85-11 shares considerable identity but the cell adhesion sites are localized in N-terminal domain and are poorly conserved (Cortez et al 2012a ), suggesting that MT and TCT molecules interact with distinct cell surface receptors, what may trigger diverse mechanisms of parasite internalization.…”

Section: Distinctive Properties Of Mt Gp82 and Tct Surfacementioning

confidence: 99%

The gp82 Surface Molecule of Trypanosoma cruzi Metacyclic Forms

Cortéz

Sobreira

Maeda

et al. 2013

Subcellular Biochemistry

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Gp82 is a surface glycoprotein expressed in Trypanosoma cruzi metacyclic trypomastigotes, the parasite forms from the insect vector that initiate infection in the mammalian host. Studies with metacyclic forms generated in vitro, as counterparts of insect-borne parasites, have shown that gp82 plays an essential role in host cell invasion and in the establishment of infection by the oral route. Among the gp82 properties relevant for infection are the gastric mucin-binding capacity and the ability to induce the target cell signaling cascades that result in actin cytoskeleton disruption and lysosome exocytosis, events that facilitate parasite internalization. The gp82 sequences from genetically divergent T. cruzi strains are highly conserved, displaying >90 % identity. Both the host cell-binding sites, as well as the gastric mucin-binding sequence of gp82, are localized in the C-terminal domain of the molecule. In the gp82 structure model, the main cell-binding site consists of an α-helix, which connects the N-terminal β-propeller domain to the C-terminal β-sandwich domain, where the second cell binding site is nested. The two cell binding sites are fully exposed on gp82 surface. Downstream and close to the α-helix is the gp82 gastric mucin-binding site, which is partially exposed. All available data support the notion that gp82 is structurally suited for metacyclic trypomastigote invasion of host cells and for initiating infection by the oral route.

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Section: Distinctive Properties Of Mt Gp82 and Tct Surfacementioning

confidence: 99%

The gp82 Surface Molecule of Trypanosoma cruzi Metacyclic Forms

Cortéz

Sobreira

Maeda

et al. 2013

Subcellular Biochemistry

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“…The SAM was formed by using 95 % 4-(methylmercapto)benzaldehyde (C 8 H 8 OS -Sigma-Aldrich). The T. cruzi Tc85 protein [26] (kindly provided by W. Colli and M. J. M. Alves, of the Institute of Chemistry, S¼o Paulo University -USP, SP, Brazil) was diluted in 0.05 mol L À1 phosphate buffer solution at pH 7.5. Positive and negative sera of Chagas disease were obtained from Diagnosis Laboratory of Faculty of Pharmaceutical Sciences (Unesp, Araraquara, SP, Brazil).…”

Section: Reagents and Solutionsmentioning

confidence: 99%

Amperometric Immunosensor for Chagas’ Disease Using Gold CD‐R Transducer

et al. 2011

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Chagas disease has been spread mainly through blood transfusion or blood components, therefore the development of a device for neglected diseases with high specificity and sensitivity is important to public health. This work describes the development of an amperometric immunosensor for determination of Chagas disease through a goldbased electrode obtained from a recordable compact disc modified with 4-(methylmercapto)benzaldehyde for the immobilization of Tc85 protein of the Trypanosoma cruzi. The immunoassays were carried out using positive and negative sera from Chagasdisease patients and immunoglobulin conjugated with peroxidase enzyme. The immunosensor presented À0.949 mA as cut-off value and was applied in sera samples.

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“…Selecionamos a proteína Tc85-11 (GenBank id: AAD13347) como um membro representativo porque é uma proteína de ligação celular pertencente ao grupo II da família das gp85/TS e foi anteriormente utilizada em estudos de nosso grupo (GIORDANO et al, 1999;MARROQUIN-QUELOPANA et al, 2004). Pesquisando no banco de dados de estrutura de proteínas RCSB-PDB (BERMAN et al, 2000), identificamos a sialidase de Trypanosoma rangeli como sendo um homólogo próximo da proteína Tc85-11 com uma estrutura terciária resolvida por difração de raios-X (ID PDB: 1WCS, PARIS et al, 2005).…”

Section: Os Peptídeos Ts9 E Fly Formam Um úNico Sítio De Ligação Ao Dunclassified

“…Elas interagem com diferentes receptores presentes na matriz extracelular e superfície celular, como a laminina (GIORDANO et al, 1994(GIORDANO et al, , 1999MARROQUIN-QUELOPANA et al, 2004), proteínas de filamentos intermediários como citoqueratina e vimentina (MAGDESIAN et al, 2001;TONELLI et al, 2010), fibronectina (OUAISSI et al, 1986), mucina (STAQUICINI et al, 2010) e receptor de procinetinina-2 (KHUSAL et al, 2015). Em estudos anteriores, foi mostrado que o peptídeo VTVTNVFLYNRPLN (denominado FLY, e derivado do motivo VTVxNVxLYNRPLN) presente na Tc-85 é um sítio de ligação de citoqueratina importante para a adesão e invasão de células pelos parasitas (MAGDESIAN et al, 2001;TONELLI et al, 2010).…”

Section: Introductionunclassified

Reconhecimento molecular na doença de chagas do ponto de vista do parasita e do hospedeiro

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Modeling the Trypanosoma cruzi Tc85-11 protein and mapping the laminin-binding site

Cited by 27 publications

References 33 publications

The gp82 Surface Molecule of Trypanosoma cruzi Metacyclic Forms

The gp82 Surface Molecule of Trypanosoma cruzi Metacyclic Forms

Amperometric Immunosensor for Chagas’ Disease Using Gold CD‐R Transducer

Reconhecimento molecular na doença de chagas do ponto de vista do parasita e do hospedeiro

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