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Activity modulation of microbial enzymes by llama (Lama glama) heavy-chain polyclonal antibodies during in vivo immune responses

Published online by Cambridge University Press:  30 September 2011

A. Ferrari ,
F. S. Weill ,
M. L. Paz ,
E. M. Cela ,
D. H. González Maglio  and
J. Leoni
A. Ferrari*
Affiliation:
Immunology Section, Department of Microbiology, Immunology and Biotechnology, Pharmacy and Biochemistry School, University of Buenos Aires, Buenos Aires, Argentina
F. S. Weill
Affiliation:
Immunology Section, Department of Microbiology, Immunology and Biotechnology, Pharmacy and Biochemistry School, University of Buenos Aires, Buenos Aires, Argentina
M. L. Paz
Affiliation:
Immunology Section, Department of Microbiology, Immunology and Biotechnology, Pharmacy and Biochemistry School, University of Buenos Aires, Buenos Aires, Argentina
E. M. Cela
Affiliation:
Immunology Section, Department of Microbiology, Immunology and Biotechnology, Pharmacy and Biochemistry School, University of Buenos Aires, Buenos Aires, Argentina
D. H. González Maglio
Affiliation:
Immunology Section, Department of Microbiology, Immunology and Biotechnology, Pharmacy and Biochemistry School, University of Buenos Aires, Buenos Aires, Argentina
J. Leoni
Affiliation:
Immunology Section, Department of Microbiology, Immunology and Biotechnology, Pharmacy and Biochemistry School, University of Buenos Aires, Buenos Aires, Argentina
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Abstract

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.

Keywords

heavy-chain antibodiescamelidsenzyme modulationβ-lactamaseaspartic protease
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animal , Volume 6 , Issue 3: 61th EAAP Annual Meeting, 2010, Heraklion, Greece: 10th International Workshop on Biology of Lactation in Farm Animals (BOLFA) and Session “Evolution of mammary gland and milk secretion: consequences for lactation in farm animals” , 27 January 2012 , pp. 510 - 517
Copyright
Copyright © The Animal Consortium 2011

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