Expression of recombinant human antibody fragments capable of inhibiting the phospholipase and myotoxic activities of Bothrops jararacussu venom

Phospholipases A 2 are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. This study used a large nonimmune human scFv library named Griffin.1 (MRC, Cambridge, UK) for selection of recombinant antibodies against antigens present i...

Full description

Saved in:
Bibliographic Details
Published in:Biochimica et biophysica acta 2006-09, Vol.1760 (9), p.1450-1457
Main Authors: Tamarozzi, M.B., Soares, S.G., Marcussi, S., Giglio, J.R., Barbosa, J.E.
Format: Article
Language:English
Subjects:
Animals
Antibodies - genetics
Antibodies - immunology
Antibodies - isolation & purification
Antibodies - metabolism
Blood Coagulation - immunology
Bothropic venom
Bothrops - metabolism
Crotalid Venoms - enzymology
Crotalid Venoms - immunology
Crotalid Venoms - toxicity
Enzyme-Linked Immunosorbent Assay
Gene Expression
Group II Phospholipases A2
Heart - drug effects
Humans
Kinetics
Mice
Myotoxin
Peptide Fragments - genetics
Peptide Fragments - immunology
Peptide Fragments - isolation & purification
Peptide Fragments - metabolism
Phage Display
Phospholipase A 2
Phospholipases A - immunology
Phospholipases A - metabolism
Phospholipases A - toxicity
Recombinant Proteins - genetics
Recombinant Proteins - immunology
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Reptilian Proteins
scFv
Solubility
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Phospholipases A 2 are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. This study used a large nonimmune human scFv library named Griffin.1 (MRC, Cambridge, UK) for selection of recombinant antibodies against antigens present in Bothrops jararacussu venom and identification of specific antibodies able to inhibit phospholipase activity. Four clones were identified as capable of inhibiting this activity in vitro. These clones were able to reduce in vivo the myotoxic activity of BthTX-I and BthTX-II PLA 2, but had no effect on the in vitro anticoagulant activity of BthTX-II. This work shows the potential of using recombinant scFv libraries in the search for antibodies that neutralize relevant venom components.
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/j.bbagen.2006.04.008