Computational Identification of Uncharacterized Cruzain Binding Sites

Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the world. As current antichagastic therapies like nifurtimox and benznidazole are highly toxic, ineffective at parasite eradication, and subject t...

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Published inPLoS neglected tropical diseases Vol. 4; no. 5; p. e676
Main Authors Durrant, Jacob D., Keränen, Henrik, Wilson, Benjamin A., McCammon, J. Andrew
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 01.05.2010
Public Library of Science (PLoS)
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ISSN1935-2735
1935-2727
1935-2735
DOI10.1371/journal.pntd.0000676

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Abstract Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the world. As current antichagastic therapies like nifurtimox and benznidazole are highly toxic, ineffective at parasite eradication, and subject to increasing resistance, novel therapeutics are urgently needed. Cruzain, the major cysteine protease of Trypanosoma cruzi, is one attractive drug target. In the current work, molecular dynamics simulations and a sequence alignment of a non-redundant, unbiased set of peptidase C1 family members are used to identify uncharacterized cruzain binding sites. The two sites identified may serve as targets for future pharmacological intervention.
AbstractList Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the world. As current antichagastic therapies like nifurtimox and benznidazole are highly toxic, ineffective at parasite eradication, and subject to increasing resistance, novel therapeutics are urgently needed. Cruzain, the major cysteine protease of Trypanosoma cruzi, is one attractive drug target. In the current work, molecular dynamics simulations and a sequence alignment of a non-redundant, unbiased set of peptidase C1 family members are used to identify uncharacterized cruzain binding sites. The two sites identified may serve as targets for future pharmacological intervention.
Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the world. As current antichagastic therapies like nifurtimox and benznidazole are highly toxic, ineffective at parasite eradication, and subject to increasing resistance, novel therapeutics are urgently needed. Cruzain, the major cysteine protease of Trypanosoma cruzi, is one attractive drug target. In the current work, molecular dynamics simulations and a sequence alignment of a non-redundant, unbiased set of peptidase C1 family members are used to identify uncharacterized cruzain binding sites. The two sites identified may serve as targets for future pharmacological intervention. Chagas disease, an infection that afflicts millions of people in Central and South America, is caused by the unicellular parasite Trypanosoma cruzi. In the chronic stage of the disease, patients' hearts are adversely affected. Chagas is the leading cause of infectious heart disease in the world. The current drugs used to treat Chagas disease are highly toxic, unable to eradiate the parasite, and subject to increasing drug resistance. Consequently, researchers are actively looking for new treatments. One attractive drug target is a Chagas protein called cruzain, which is required for the parasite's survival. Drugs that can inhibit the correct functioning of cruzain within the parasite may one day serve as powerful treatments in the fight against this devastating tropical disease. To design drugs that will be effective against cruzain, we need to know what portions of the protein are crucial for its functionality. For example, portions of the protein that bind to other proteins or to small molecules are likely to be critical. These regions are called “binding sites.” In the current work, we identify two uncharacterized cruzain binding sites. With this knowledge in hand, future researchers may be able to design drugs that target these sites.
Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the world. As current antichagastic therapies like nifurtimox and benznidazole are highly toxic, ineffective at parasite eradication, and subject to increasing resistance, novel therapeutics are urgently needed. Cruzain, the major cysteine protease of Trypanosoma cruzi, is one attractive drug target. In the current work, molecular dynamics simulations and a sequence alignment of a non-redundant, unbiased set of peptidase C1 family members are used to identify uncharacterized cruzain binding sites. The two sites identified may serve as targets for future pharmacological intervention.Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the world. As current antichagastic therapies like nifurtimox and benznidazole are highly toxic, ineffective at parasite eradication, and subject to increasing resistance, novel therapeutics are urgently needed. Cruzain, the major cysteine protease of Trypanosoma cruzi, is one attractive drug target. In the current work, molecular dynamics simulations and a sequence alignment of a non-redundant, unbiased set of peptidase C1 family members are used to identify uncharacterized cruzain binding sites. The two sites identified may serve as targets for future pharmacological intervention.
  Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the world. As current antichagastic therapies like nifurtimox and benznidazole are highly toxic, ineffective at parasite eradication, and subject to increasing resistance, novel therapeutics are urgently needed. Cruzain, the major cysteine protease of Trypanosoma cruzi, is one attractive drug target. In the current work, molecular dynamics simulations and a sequence alignment of a non-redundant, unbiased set of peptidase C1 family members are used to identify uncharacterized cruzain binding sites. The two sites identified may serve as targets for future pharmacological intervention.
Author Wilson, Benjamin A.
Keränen, Henrik
Durrant, Jacob D.
McCammon, J. Andrew
AuthorAffiliation 2 Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, Uppsala, Sweden
McGill University, Canada
5 Department of Chemistry & Biochemistry, National Science Foundation Center for Theoretical Biological Physics, National Biomedical Computation Resource, University of California San Diego, La Jolla, California, United States of America
4 Department of Ecology & Evolutionary Biology, University of Arizona, Tucson, Arizona, United States of America
1 Biomedical Sciences Program, University of California San Diego, La Jolla, California, United States of America
7 Howard Hughes Medical Institute, University of California San Diego, La Jolla, California, United States of America
3 University of California San Diego, La Jolla, California, United States of America
6 Department of Pharmacology, University of California San Diego, La Jolla, California, United States of America
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– name: McGill University, Canada
– name: 4 Department of Ecology & Evolutionary Biology, University of Arizona, Tucson, Arizona, United States of America
– name: 5 Department of Chemistry & Biochemistry, National Science Foundation Center for Theoretical Biological Physics, National Biomedical Computation Resource, University of California San Diego, La Jolla, California, United States of America
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ContentType Journal Article
Copyright 2010 Durrant et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Durrant JD, Keränen H, Wilson BA, McCammon JA (2010) Computational Identification of Uncharacterized Cruzain Binding Sites. PLoS Negl Trop Dis 4(5): e676. doi:10.1371/journal.pntd.0000676
Durrant et al. 2010
Copyright_xml – notice: 2010 Durrant et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Durrant JD, Keränen H, Wilson BA, McCammon JA (2010) Computational Identification of Uncharacterized Cruzain Binding Sites. PLoS Negl Trop Dis 4(5): e676. doi:10.1371/journal.pntd.0000676
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Issue 5
Keywords Cysteine Endopeptidases
Antiprotozoal Agents
Protease Inhibitors
Computational Biology
Models, Molecular
Protein Binding
Protozoan Proteins
Binding Sites
Trypanosoma cruzi
Language English
License This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
cc-by
Creative Commons Attribution License
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Conceived and designed the experiments: JDD BAW. Performed the experiments: JDD HK BAW. Analyzed the data: JDD HK BAW. Contributed reagents/materials/analysis tools: JAM. Wrote the paper: JDD HK BAW JAM.
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PublicationTitle PLoS neglected tropical diseases
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Snippet Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the...
  Chagas disease, caused by the unicellular parasite Trypanosoma cruzi, claims 50,000 lives annually and is the leading cause of infectious myocarditis in the...
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SubjectTerms Antiprotozoal Agents - metabolism
Binding Sites
Biochemistry/Drug Discovery
Biochemistry/Theory and Simulation
Biologi
Biology
Computational Biology - methods
Computational Biology/Comparative Sequence Analysis
Computational Biology/Molecular Dynamics
Cysteine Endopeptidases - genetics
Infections
Infectious Diseases/Neglected Tropical Diseases
Infectious Diseases/Protozoal Infections
Medical research
MEDICIN
MEDICINE
Models, Molecular
NATURAL SCIENCES
NATURVETENSKAP
Parasites
Protease Inhibitors - metabolism
Protein Binding
Proteins
Protozoan Proteins - antagonists & inhibitors
Protozoan Proteins - genetics
Tropical diseases
Trypanosoma cruzi - enzymology
Vector-borne diseases
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Title Computational Identification of Uncharacterized Cruzain Binding Sites
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