Human Single-Chain Antibodies That Neutralize Elastolytic Activity of Pseudomonas aeruginosa LasB

Isolation of human monoclonal antibodies that neutralize human rotavirus.

A human antibody library constructed by utilizing a phage display system was used for the isolation of human antibodies with neutralizing activity specific for human rotavirus. In the library, the Fab form of an antibody fused to truncated cp3 is expressed on the phage surface. Purified virions of strain KU (G1 serotype and P[8] genotype) were used as antigen. Twelve different clones were isola...

Single Domain Camelid Antibodies that Neutralize Negative Strand Viruses

Analysis of the Pseudomonas aeruginosa elastase (lasB) regulatory region.

The enzyme elastase is an important virulence factor of the opportunistic human pathogen Pseudomonas aeruginosa. Previous studies have shown that expression of the P. aeruginosa elastase gene (lasB) requires both an activator protein, LasR, and an N-acylhomoserine lactone compound termed Pseudomonas autoinducer (PAI). In this study, we analyzed the lasB promoter region to learn more about lasB ...

Comparison of two single-chain antibodies that neutralize canine parvovirus: analysis of an antibody-combining site and mechanisms of neutralization.

We cloned the heavy- and light-chain variable domains of two monoclonal antibodies that recognize each of the two major neutralizing antigenic sites of the canine parvovirus (CPV) capsid. After expression in Escherichia coli as single-chain variable domains (scFv) with glycine-serine linker sequences, both scFv bound CPV capsids with the same specificity as the intact IgG, but with 10- to 20-fo...

EXTRACELLULAR LIPA SE ACTIVITY CHARACTERIZATION OF SOME PSEUDOMONAS AERUGINOSA STRA INS ISOLATED FROM HUMAN INFECTIONS

Pseudomonas aeruginosa EF2, ATCC 9027 and ATCC 19660 were grown in a continuous culture under Tween 80 (polyoxyethylene sorbitan monooleate) limitation and optimum conditions (pH 6.5, 37°C at dilution rate of 0.05/h). Culture supernatants were carefully removed and stored at -20°C. To purify the lipases, the culture supernatant was reduced in volume to approximately 10 mL by an ultrafiltra...