Walter Colli

ORCID: 0000-0001-7305-4673
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About
Contact & Profiles
Research Areas
  • Trypanosoma species research and implications
  • Research on Leishmaniasis Studies
  • Carbohydrate Chemistry and Synthesis
  • Biochemical and Molecular Research
  • Lysosomal Storage Disorders Research
  • Glycosylation and Glycoproteins Research
  • Toxin Mechanisms and Immunotoxins
  • Synthesis and Biological Evaluation
  • Galectins and Cancer Biology
  • RNA and protein synthesis mechanisms
  • Monoclonal and Polyclonal Antibodies Research
  • Bacterial Genetics and Biotechnology
  • Calcium signaling and nucleotide metabolism
  • DNA and Nucleic Acid Chemistry
  • Vector-Borne Animal Diseases
  • Viral Infections and Immunology Research
  • Advanced biosensing and bioanalysis techniques
  • Science and Science Education
  • Parasitic Infections and Diagnostics
  • Studies on Chitinases and Chitosanases
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Bacteriophages and microbial interactions
  • Helminth infection and control
  • Polyamine Metabolism and Applications
  • Insect symbiosis and bacterial influences

Universidade de São Paulo
2013-2025

Directorate-General for Research and Innovation
2016

Fundação de Amparo à Pesquisa do Estado de São Paulo
2016

European Commission
2016

Inserm
2016

National Research Foundation of Korea
2016

South African Medical Research Council
2016

Canadian Institutes of Health Research
2016

Universidade Cidade de São Paulo
2014

Instituto de Botânica
2003-2008

A quantitative method for experimentally separating the adhesion and interiorization phases of interaction Trypanosoma cruzi with mammalian cells was developed. Incubation confluent monolayers epimastigotes or trypomastigotes at 4 degrees C allowed evaluation number adhered parasites that do not become interiorized this temperature. Quantification 34 achieved by employing hypotonic lysis to eliminate extracellularly trypomastigotes. Both were found be proportional time exposure multiplicity...

10.1111/j.1550-7408.1982.tb04024.x article EN The Journal of Protozoology 1982-05-01

Trypomastigote forms of Trypanosoma cruzi, the causative agent Chagas Disease, shed extracellular vesicles (EVs) enriched with glycoproteins gp85/trans-sialidase (TS) superfamily and other α-galactosyl (α-Gal)-containing glycoconjugates, such as mucins. Here, purified from T. cruzi strains (Y, Colombiana, CL-14 YuYu) were quantified according to size, intensity concentration. Qualitative analysis revealed differences in their protein contents. Later, those polymorphisms evaluated modulation...

10.3402/jev.v4.28734 article EN cc-by-nc Journal of Extracellular Vesicles 2015-01-01

Trypanosoma cruzi causing Chagas' disease needs to invade host cells complete its life cycle. Macromolecules on cell surfaces such as laminin, thrombospondin, heparan sulfate, and fibronectin are believed be important in mediating parasite-host adhesions the invasion process of by parasite. The SELEX technique (systematic evolution ligands byexponential enrichment) was used evolve nuclease-resistant RNA (aptamer = fit) that bind with affinities 40–400 nm parasite receptors for matrix...

10.1074/jbc.m111859200 article EN cc-by Journal of Biological Chemistry 2002-06-01

Using as the host cell, a proline-requiring mutant of Chinese hamster ovary cell (CHO-K1), it was possible to arrest differentiation amastigote forms Trypanosoma cruzi at intermediate intracellular epimastigote-like stage. Complete trypomastigote stage obtained by addition l-proline medium. This effect more pronounced using T. CL-14 clone that differentiates fully 33°C (permissive temperature) and poorly 37°C (restrictive temperature). A synchronous inside host-cell is then temperature...

10.1111/j.1462-5822.2004.00397.x article EN Cellular Microbiology 2004-05-04

Gold nanoparticle (AuNP) bioconjugates have been used as therapeutic and diagnostic tools; however, in vivo biocompatibility cytotoxicity continue to be two fundamental issues. The effect of AuNPs (20 nm) conjugated with antibody [immunoglobulin G (IgG)], albumin, protein A, PEG4000, citrate (cit) were evaluated vitro using primary human cells the vascular system. AuNP did not cause lysis erythrocytes, apoptosis or necrosis leukocytes, endothelial vitro, although had internalized detected...

10.1093/toxsci/kfu202 article EN Toxicological Sciences 2014-09-25

The infective trypomastigote stage ofTrypanosoma cruzi expresses a set of surface glycoproteins that are known collectively as Tc85 and belong to the gp85/trans-sialidase supergene family. A member this family, Tc85–11, with adhesive properties laminin cell surfaces was recently cloned. In report, Tc85–11 domain for binding its corresponding receptor on epithelial LLC-MK2are described. Using synthetic peptides carboxyl-terminal segment, we show mammalian cell-binding colocalizes most...

10.1074/jbc.m011474200 article EN cc-by Journal of Biological Chemistry 2001-06-01

Trypanosoma cruzi, the agent of Chagas' disease, alternates between different morphogenetic stages that face distinct physiological conditions in their invertebrate and vertebrate hosts, likely availability glucose. While glucose transport is well characterized epimastigotes T. nothing known about how mammalian acquire this molecule. Herein activity expression were analyzed three developmental present cycle cruzi. The infective trypomastigotes showed highest (V(max)=5.34+/-0.54 nmol/min per...

10.1016/j.molbiopara.2009.07.006 article EN publisher-specific-oa Molecular and Biochemical Parasitology 2009-07-24

10.1016/0304-4165(76)90226-9 article EN Biochimica et Biophysica Acta (BBA) - General Subjects 1976-08-01

SYNOPSIS Epimastigotes of Trypanosoma cruzi obtained in culture agglutinate readily with low concentrations concanavalin A (Con A). Agglutination was linear time up to 10 min providing that the initial cell density greater than 1 × 8 cells/ml. Under these conditions, percentage agglutination dependent on Con concentration. inhibited by α‐methyl D‐mannoside, α‐D‐mannose, and α‐D‐glucose. Pretreatment cells trypsin had no effect epimastigote agglutinations. Blood forms (trypomastigotes) T. did...

10.1111/j.1550-7408.1974.tb03704.x article EN The Journal of Protozoology 1974-10-01
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