Heat treatment of bovine colostrum: II. Effects on calf serum immunoglobulin, insulin, and IGF-I concentrations, and the serum proteome

Abstract

In-depth analysis of colostrum components has identified hundreds of proteins, but data are sparse regarding their systemic uptake in the newborn calf. Moreover, heat treatment may influence these colostral components and their absorption. Our objectives were to describe the serum proteome of newborn calves before and after colostrum feeding and the possible effects of colostral heat treatment. Newborn Holstein heifer calves (n = 22) were randomized within pair and fed heat-treated (n = 11; 60°C, 60 min) or raw (n = 11) colostrum at 8.5% of birth body weight by esophageal feeder within 1 h of birth. After the single colostrum feeding, calves were not fed until after the 8-h time point, when milk was offered free-choice. Blood samples were taken immediately before feeding (0 h), as well as 4, 8, and 24 h after feeding. Whole blood packed cell volume (%), serum Brix percentage, and plasma glucose concentrations were determined for all time points. Plasma insulin and insulin-like growth factor-I concentrations were determined by radioimmunoassay for selected time points. Serum IgA and IgG were measured by radial immunodiffusion at 24 h. The serum proteome was analyzed using nano-scale reverse-phase chromatography and tandem mass spectrometry (nano LC-MS/MS) in 0-and 8-h samples. For proteomics analysis, ratios of results for 8-h to 0-h samples were analyzed with false discovery rate adjustment. For all other outcomes, repeated-measures ANOVA was performed with the fixed effects of group, time, and their interaction, and random effect of pair. Serum Brix percentage and glucose concentrations increased over time and were independent of colostrum treatment. Serum IgG and IgA concentrations at 24 h did not differ between groups. Nano LC-MS/MS identified a total of 663 unique proteins in serum, of which 261 increased in abundance, whereas 67 decreased in abundance after feeding in both groups. Among serum proteins that increased in abundance and that were previously identified in colostrum, many belonged to those involved in immune response, coagulation, the classical complement pathway, or the antimicrobial peptide class of cathelicidins. Serum proteins that decreased in abundance and that were identified in colostrum belonged to the alternative complement pathway and the membrane attack complex. Thirty-eight proteins differed in calves that were fed heat-treated colostrum compared with those fed raw colostrum. Decreased abundances in calves fed heat-treated colostrum included several enzymes involved in glycolysis or glycogenolysis, whereas the incretin gastric inhibitory polypeptide and serum insulin were increased in this group. Our findings point to important innate immune defense pathways associated with colostrum ingestion in newborn calves. Furthermore, calves fed heat-treated colostrum showed differences in serum proteins and enzymes associated with carbohydrate metabolism.

Current Diagnostic Methods for Assessing Transfer of Passive Immunity in Calves and Possible Improvements: A Literature Review

“…Zhang et al [64] identified 212 different types of proteins in the colostrum and milk proteome of four cows and quantified 208 of the identified proteins. Mann et al [65] identified 663 different kinds of proteins, while using proteomics techniques to evaluate the serum proteins with a low abundance in newborn calves. However, although Mann et al [65] measured IgG using RID, the authors did not quantify IgG using the proteome.…”

A Scoping Review of On-Farm Colostrum Management Practices for Optimal Transfer of Immunity in Dairy Calves

“…Indeed, viability was reduced but not completely eliminated after pasteurizing for 60 min at 60°C. Also the authors state that although viability of colostral immune cells is reduced, more research is required regarding functionality and biological meaning of colostral cells ( 45 ).…”

“…We summarized the results of the existing literature in Supplementary Table 1. The majority of studies show that colostral IgG concentration is not (41)(42)(43)(44)(45)(46)(47)(48)(49)(50)(51)(52)(53) or only slightly affected (54-57) by heating at <60 • C for either 30 or 60 min. In contrast, heating of colostrum above 60 • C frequently resulted in significant loss of colostral IgG (41-48, 50, 54, 58-60).…”

Influence of first colostrum pasteurization on serum immunoglobulin G, iron, and activity of gamma-glutamyltransferase in newborn dairy calves

“…This observation can be explained by the heat stability of different proteins. In general, the heating of colostrum results in a change in the solubility of almost all whey proteins, an effect that can be observed at temperatures as low as 40°C [35,36]. Gradual denaturation of proteins occurs at temperatures of 60°C and higher due to the destruction of the secondary or tertiary structure caused by the dissolution of non-covalent bonds [37].…”