Science and Technology Production
Article
Authorship
Alejandro Ferrari
;
Federico S. Weill
;
PAZ, MARIELA LAURA
;
Eliana M Cela
;
Daniel H. González Maglio
;
Juliana Leoni
Date
2011
Publishing House and Editing Place
CAMBRIDGE UNIV PRESS
Magazine
ANIMAL
(pp. 1-8)
CAMBRIDGE UNIV PRESS
Summary
Information provided by the agent in
SIGEVA
Since they were first described in 1993, it was found that recombinant variable fragments (rVHHs) of heavy-chain antibodies (HCAbs) from Camelidae have unusual biophysical properties, as well as a special ability to interact with epitopes that are cryptic for conventional Abs. It has been assumed that in vivo raised polyclonal HCAbs (pHCAbs) should behave in a similar manner than rVHHs; however, this assumption has not been tested sufficiently. Furthermore, our own preliminary work on a single ...
Since they were first described in 1993, it was found that recombinant variable fragments (rVHHs) of heavy-chain antibodies (HCAbs) from Camelidae have unusual biophysical properties, as well as a special ability to interact with epitopes that are cryptic for conventional Abs. It has been assumed that in vivo raised polyclonal HCAbs (pHCAbs) should behave in a similar manner than rVHHs; however, this assumption has not been tested sufficiently. Furthermore, our own preliminary work on a single serum sample from a llama immunized with a β-lactamase, has suggested that pHCAbs have no special ability to down-modulate catalytic activity. In this work, we further explored the interaction of pHCAbs from four llamas raised against two microbial enzymes and analyzed it within a short and a long immunization plan. The relative contribution of pHCAbs to serum titer was found to be low compared with that of the most abundant conventional subisotype (IgG1), during the whole immunization schedule. Furthermore, pHCAbs not only failed to inhibit the enzymes, but also activated one of them. Altogether, these results suggest that raising high titer inhibitory HCAbs is not a straightforward strategy – neither as a biotechnological strategy nor in the biological context of an immune response against infection – as raising inhibitory rVHHs.
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Key Words
BETA-LACTAMASEENZYME MODULATIONCAMELIDSHEAVY CHAIN ANTIBODIESASPARTIC PROTEASE