Abstract：
:We aimed to identify antibodies that can recognize the Asn-Xaa-Ser/Thr(NXS/T) N-glycosylation site that guides oligosaccharyltransferase (OT) activity. We used synthetic Asn-Cys-Ser/Thr(NCS/T) tripeptides conjugated to bovine serum albumin to isolate single chain antibody fragments of a variable region (scFv) from the Griffin 1 phage antibody library. Although Ser and Thr have different side chains, the scFv proteins thus isolated bound to both NCS and NCT with Kd values of the order of 10(-6) M and accepted the substitution of the Cys residue with various amino acids, including Ala, Gly, and Val. However, these proteins recognized neither Asn-Pro-Ser/Thr nor non-NXS/T tripeptides. The scFv proteins recognized NCS/T and N-glycosylation site of mutant yeast protein disulfide isomerase when they were in their native but not denatured state. These results indicate that antibody recognition of the NXS/T motif is conformation dependent and suggest that NXS/T spontaneously adopts a specific conformation that is necessary for antibody recognition. These features are likely to correlate with the known binding specificity of OT.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Kikuchi M,Kataoka M,Kojima T,Horibe T,Fujieda K,Kimura T,Tanaka Tdoi
10.1016/j.abb.2003.12.032subject
Has Abstractpub_date
2004-02-15 00:00:00pages
221-9issue
2eissn
0003-9861issn
1096-0384pii
S0003986103007045journal_volume
422pub_type
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