A consensus peptide sequence, QSYP, appears as an artifact during the mapping of monoclonal antibodies (MAbs) using a random peptide phage display library. Phage bearing this QSYP sequence were independently selected by four different laboratories screening separate MAb preparations with the same phage library. In each case, the QSYP sequence was selected in addition to a consensus sequence specific to the MAb. Phage that displayed the QSYP sequence were not bound by the MAb of interest, but rather bound to bovine IgG derived from the FBS present in the hybridoma growth media. The implications of this finding for the interpretation of phage library screening results and possible methods for the removal of bovine IgG from MAb preparations are discussed.
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http://dx.doi.org/10.2144/03341rr04 | DOI Listing |
J Anim Sci Biotechnol
January 2025
Center for Animal Nutrition and Welfare, University of Veterinary Medicine Vienna, Veterinärplatz 1, 1210, Vienna, Austria.
Background: The objective was to characterize the colostrum proteome of primiparous Holstein cows in association with immunoglobulin G (IgG) content. Immediately after calving, colostrum samples were collected from 18 cows to measure IgG concentration. Based on colostrum IgG content, samples were classified through cluster analysis and were identified as poor, average, and excellent quality.
View Article and Find Full Text PDFNPJ Vaccines
January 2025
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Australia.
Cyclic peptides are often used as scaffolds for the multivalent presentation of drug molecules due to their structural stability and constrained conformation. We identified a cyclic deca-peptide incorporating lipoamino acids for delivering T helper and B cell epitopes against group A Streptococcus (GAS), eliciting robust humoral immune responses. In this study, we assessed the function-immunogenicity relationship of the multi-component vaccine candidate (referred to as VC-13) to elucidate a mechanism of action.
View Article and Find Full Text PDFAnaerobe
January 2025
Centro de Desenvolvimento Tecnológico, Biotecnologia, Universidade Federal de Pelotas, Rio Grande do Sul, Brazil.
Paeniclostridium sordellii is responsible for severe infections in horses, cattle, and sheep, however, conventional vaccines exhibit limitations in production and immunogenicity. This study assessed the immunogenicity of a recombinant bacterin composed of a chimera (rQTcsHL) that combines segments from the lethal (TcsL) and hemorrhagic (TcsH) toxins in mice and sheep. Both immunized animal groups exhibited elevated levels of IgG, with the mice demonstrating moderate protection (<50 %) against lethal challenges, comparable to that of the conventional vaccine.
View Article and Find Full Text PDFJ Dairy Sci
January 2025
Department of Agronomy, Food, Natural resources, Animals and Environment, University of Padova, Viale dell'Università 16, 35020 Legnaro (PD), Italy.
The quality of bovine colostrum, primarily determined by IgG concentration, is essential for the transfer of passive immunity and the development of the gastrointestinal tract in neonates. High IgG concentration in bovine colostrum (BC) is pivotal for the calf at first meal; however, while neonates often refuse to voluntarily drink the recommended amount of BC in the first hours of life, the dam frequently fails to produce a sufficient volume of colostrum at first milking. This study seeks to estimate the h of colostrum yield (CY) and its genetic correlations with total Ig, IgG, protein, and fat concentrations for the first time in the Italian Holstein population.
View Article and Find Full Text PDFJ Agric Food Chem
January 2025
State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, China.
Milk proteins possess an abundance of free amino groups and exhibit diverse spatial structures. During food processing, these properties facilitate their interaction with hydrophobic ligands, such as linolenic acid. Exploring the IgE and IgG binding ability of linolenic acid-milk protein complexes at different temperatures, times, and molar ratios is crucial for controlling the allergenicity of milk proteins in food processing.
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