IN antibodies, a heavy and a light chain variable domain, VH and VL, respectively, pack together and the hypervariable loops on each domain contribute to binding antigen1–4. We find, however, that isolated VH domains with good antigen-binding affinities can also be prepared. Using the polymerase chain reaction5, diverse libraries of VH genes were cloned from the spleen genomic DNA of mice immunized with either lysozyme or keyhole-limpet haemocyanin. From these libraries, VH domains were expressed and secreted from Escherichia coli. Binding activities were detected against both antigens, and two VH domains were characterized with affinities for lysozyme in the 20 nM range. Isolated variable domains may offer an alternative to monoclonal antibodies and serve as the key to building high-affinity human antibodies. We suggest the name 'single domain antibodies (dAbs)' for these antigen binding demands.

Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli

CONTENTS INTRODUCTION . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 61 FIVE CHEMICALLY DIFFERENT GROUPS OF PEPTIDE ANTIBIOTICS . . . . . . . . . . .. 63 Linear, Mostly Helical, Peptides Without Cys, With or Without a Hinge . . . . . . . . . . . . . . . 63 Linear Pep tides Without Cys and with a High Proportion of Certain Residues . . . . . . . . . 67 Antibacterial Peptides with One Disulfide Bond . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 68 Peptides with Two or More S-S Bonds Giving Mainly or Only fJ-Sheet Structures. . . . . . . 69 Antibacterial Peptides Derivedfrom Larger Polypeptides with Other Known Functions . . 72 ANTIBACTERIAL PROTEINS AND ACTIVE FRAGMENTS OF SUCH PROTEINS . . . . 73

Peptide antibiotics and their role in innate immunity.

http://compbio.korea.ac.kr/wiki/images/8/83/Mmbr.1996.expression.pdf

Strategies for achieving high-level expression of genes in Escherichia coli.

A chimeric mouse-human Fab protein that binds specifically to the human carcinoma cell line C3347 has been expressed and secreted from Escherichia coli This molecule, which contains functionally assembled kappa and Fd proteins, binds as effectively to sites on the surface of C3347 cells as Fab fragments prepared proteolytically from whole chimeric or mouse antibody The production in Escherichia coli of foreign heterodimeric protein reagents, such as Fab, should prove useful in the management of human disease

https://science.sciencemag.org/content/sci/240/4855/1041.full.pdf

Escherichia coli secretion of an active chimeric antibody fragment

Modular assembly of antibody genes, antibodies prepared thereby and use.

The pelB gene encodes pectate lyase B, one of three pectate lyases identified in Erwinia carotovora EC. Pectate lyase B was purified from Escherichia coli containing the pelB gene on a recombinant plasmid. The activity of the protein was optimal at a pH of 8.3. The amino acid composition, N-terminal amino acid sequence, and C-terminal peptide sequence were determined and compared with the polypeptide sequence deduced from the DNA sequence of pelB. Purified pectate lyase B started at amino acid 23 of the predicted sequence, suggesting that a 22-amino-acid leader peptide had been removed. Pectate lyase B of E. carotovora EC and pectate lyase B of E. chrysanthemi EC16 contain 352 and 353 amino acids, respectively (N. T. Keen, S. Tanaki, W. Belser, D. Dahlbeck, and B. Staskawicz, J. Bacteriol. 168:595-606, 1986). The two proteins are 72% homologous on the basis of DNA sequence data, and 75% of the amino acids are identical.

Characterization of the Erwinia carotovora pelB gene and its product pectate lyase.

Cecropin A is a naturally occurring peptide with bactericidal activity against gram-negative and gram-positive bacteria. Production of large quantities of bactericidal peptides that are similar in structure and activity to cecropin A has been achieved by combining recombinant DNA techniques and techniques and chemical modification. Expression of the bactericidal peptide in Escherichia coli was accomplished through the formation of a fusion protein. The 5' end of the L-ribulokinase gene was fused to a single copy of a synthetic gene encoding cecropin A. A methionine codon was engineered between the two genes, and a methionylglycine extension was introduced at the C terminus of cecropin A. Cyanogen bromide treatment of the fusion protein yielded cecropin A with a C-terminal homoserine. The recombinant cecropin A with a homoserine at the C terminus did not kill most gram-positive bacteria tested. However, recombinant cecropin A with a chemically modified C terminus has antimicrobial activity similar to that of cecropin produced by cecropia pupae.

Modification of the C terminus of cecropin is essential for broad-spectrum antimicrobial activity.

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Characterization of the Erwinia carotovora pelB gene and its product pectate lyase.

Modification of the C terminus of cecropin is essential for broad-spectrum antimicrobial activity.