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At least 937 records · Page 52Linked to original sources
PubMed2005

Engineering camel single-domain antibodies and immobilization chemistry for human prostate-specific antigen sensing.

The specificity and affinity characteristics of antibodies make them excellent probes in biosensor applications. Unfortunately, their large size, unstable behavior, and random immobilization properties create numerous problems. The single-domain antigen-binding fragment derived from heavy-chain antibodies of camelids (termed VHH) offers special advantages in terms of size, stability, and ease of generating different antibody constructs. In this study, we show the potential of those VHHs in sensing human prostate-specific antigen (hPSA) by SPR technology. Different VHH constructs were immobilized onto commercial and custom-built sensor surfaces by metal chelation, biotin-streptavidin interaction, or covalent coupling. The detection of subnanogram per milliliter hPSA concentrations could be attained on a covalently coupled three-dimensional dextran surface. Moreover, the ratio of different hPSA isoform concentrations could be assessed via a sandwich assay and resulted in the detection of clinically significant antigen concentrations within 15 min. In addition, for the first time, the intrinsic protein stability is presented as an important probe design factor, since our results reveal that higher intrinsic stability offers higher resistance to harsh regeneration conditions. In conclusion, we present VHHs as a novel class of biosensor probes rivaling conventional antibodies and their derived antibody fragments.

Animals↗
PubMed1998

Traffic of the tick embryo basic protein during embryogenesis of the camel tick Hyalomma dromedarii (Acari: Ixodidae).

The tick embryo basic protein (TEBP) is present in the nucleus as a counterpart of histones at early embryonic stages of the tick Hyalomma dromedarii. The sharp drop in the TEBP nuclear level and elimination of the N-terminal dipeptide (leucine-serine) between days 12 and 15 after oviposition suggested the transport of TEBP to the cytoplasm for protein turnover. The traffic of TEBP during tick embryogenesis was examined. The level of TEBP was detected in the cytoplasm from the different embryonic stages by the established enzyme-linked immunosorbent assay (ELISA) and confirmed by immunoblotting. At day 12, a 2-fold increase in the cytoplasmic TEBP level coincided with its decrease in the nucleus. This result indicates that TEBP starts to leave the nucleus for the cytoplasm at day 12. The changes in the cytoplasmic leucine aminopeptidase (LAP)-specific activity were followed during tick embryogenesis. The LAP activity started to increase at day 12 and reached its maximum level at day 21. The enzyme displayed an optimum pH between 7.5 and 8.8 and a K(m) value of 0.5 microM for leucine-p-nitroanilide. The involvement of the exopeptidase activity in the TEBP turnover after its translocation to the cytoplasm is discussed.

Amino Acid Sequence↗