ArticlePloS one2008
Relevance of the diversity among members of the Trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Camelid Single-Domain Antibodies as Tools for Novel Target Identification in Kinetoplastid Research.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Asymmetric bifunctional protein nanoparticles through redesign of self-assembly.Nanoscale advances · 2019Article
- Adenylate Cyclases ofPathogens (Basel, Switzerland) · 2018Review
- Camelid Single-Domain Antibodies As an Alternative to Overcome Challenges Related to the Prevention, Detection, and Control of Neglected Tropical Diseases.Frontiers in immunology · 2017Review
- Improved proteomic approach for the discovery of potential vaccine targets in Trypanosoma cruzi.Journal of proteome research · 2012Article
- Immunodiagnosis of neurocysticercosis: ways to focus on the challenge.Journal of biomedicine & biotechnology · 2011Review
- Article
- Continuous nonradioactive method for screening trypanosomal trans-sialidase activity and its inhibitors.Glycobiology · 2010Article
- A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic alpha-exosite binding region.Journal of molecular biology · 2010Article
- Single domain antibodies: promising experimental and therapeutic tools in infection and immunity.Medical microbiology and immunology · 2009Review
- Two approaches to discovering and developing new drugs for Chagas disease.Memorias do Instituto Oswaldo Cruz · 2009Article
- Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The sialic acid present in the protective surface mucin coat of Trypanosoma cruzi is added by a membrane anchored trans-sialidase (TcTS), a modified sialidase that is expressed from a large gene family. In this work, we analyzed single domain camelid antibodies produced against trans-sialidase. Llamas were immunized with a recombinant trans-sialidase and inhibitory single-domain antibody fragments were obtained by phage display selection, taking advantage of a screening strategy using an inhibition test instead of the classic binding assay. Four single domain antibodies displaying strong trans-sialidase inhibition activity against the recombinant enzyme were identified. They share the same complementarity-determining region 3 length (17 residues) and have very similar sequences. This result indicates that they likely derived from a unique clone. Probably there is only one structural solution for tight binding inhibitory antibodies against the TcTS used for immunization. To our surprise, this single domain antibody that inhibits the recombinant TcTS, failed to inhibit the enzymatic activity present in parasite extracts. Analysis of individual recombinant trans-sialidases showed that enzymes expressed from different genes were inhibited to different extents (from 8 to 98%) by the llama antibodies. Amino acid changes at key positions are likely to be responsible for the differences in inhibition found among the recombinant enzymes. These results suggest that the presence of a large and diverse trans-sialidase family might be required to prevent the inhibitory response against this essential enzyme and might thus constitute a novel strategy of T. cruzi to evade the host immune system.
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