relevance of the diversity among members of the trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies相关性之间的多样性与骆驼科鲁兹锥体trans-sialidase家族成员分析了单极抗体.pdfVIP
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relevance of the diversity among members of the trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies相关性之间的多样性与骆驼科鲁兹锥体trans-sialidase家族成员分析了单极抗体
Relevance of the Diversity among Members of the
Trypanosoma Cruzi Trans-Sialidase Family Analyzed with
Camelids Single-Domain Antibodies
1. 2. ´ 2 2¤ 1
Laura Ratier , Mariela Urrutia , Gaston Paris , Laura Zarebski , Alberto C. Frasch *, Fernando A.
Goldbaum2*
´ ´ ´ ´
1 Instituto de Investigaciones Biotecnologicas-Instituto Tecnologico de Chascomus (IIB-INTECH), Universidad Nacional de General San Martın-CONICET, Buenos Aires,
´ ´
Argentina, 2 Fundacion Instituto Leloir, Instituto de Investigaciones Bioquımicas Buenos Aires-CONICET, Buenos Aires, Argentina
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 in
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