Open AccessNeutralising human recombinant antibodies to human cytomegalovirus glycoproteins gB and gH
Author(s) -
Nejatollahi Foroogh,
Hodgetts Samantha J,
Vallely Pamela J,
Burnie James P
Publication year - 2002
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.2002.tb00630.x
Subject(s) - phage display , antibody , glycoprotein , recombinant dna , biology , human cytomegalovirus , microbiology and biotechnology , epitope , virology , peptide library , immunoglobulin light chain , clone (java method) , peptide sequence , peptide , biochemistry , genetics , virus , gene
A phage antibody display library of single chain fragment variable (scFv) was applied to develop anti‐HCMV glycoprotein B (gB) and glycoprotein H (gH) neutralising libraries. To enrich for specific scFvs, the phage antibody was panned against cytomegalovirus epitopes derived from the N‐terminal part of gB, the C‐terminal part of gB and the N‐terminal part of gH (NETIYNTTLKYGDV, VTSGSTKD and AASEALDPHAFHLLLNTYGR). A number of clones were differentiated by Bst N1 fingerprinting. After isolation of specific clones against each peptide, the neutralising effect of each clone was assessed by plaque reduction assay. This resulted in the isolation of eight neutralising scFv antibodies with 51–63% neutralising effects. Sequence analysis of three neutralising clones revealed the amino acids specificity changes in heavy and light chains of antibody molecules.