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Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Antibodies to Escherichia coli and Shigella flexneri in milk from undernourished mothers: studies on sodium dodecyl sulfate-polyacrylamide gel electrophoresis-separated antigens.
Pediatric Research 1997 November
Analysis of IgA, IgM, and IgG antibodies against Escherichia coli O6, its lipopolysaccharide (LPS), and Shigella flexneri were performed in the milk of moderately undernourished Guatemalan women receiving either a low or a high calorie supplement, using SDS-PAGE. As expected, the immunostaining analysis of milk antibodies showed that IgA was the predominant isotype in both groups. Concerning the other Igs, antibodies against O6 LPS were mainly of the IgM isotype, whereas IgG antibodies were more prominent than IgM against the bacterial whole cell preparations. Seven to nine distinct bands, ranging in molecular mass from 13.5 to 109 kD were selected for each antigen to compare the milk antibodies between the two groups of women. After a 20-wk supplementation period, the IgA and IgG antibodies to the E. coli, O6 LPS, and S. flexneri were not found negatively affected by a low calorie intake. A significantly lower immunostaining intensity was, however, obtained for the low calorie intake group regarding the IgM antibody activity against four high molecular mass bands of the E. coli whole cell preparation. A decreased immunostaining intensity was also found in the same group for IgM antibodies against two bands of E. coli O6 LPS when analyzing paired samples collected at d 0 and wk 20. No differences were found for IgM antibodies against any of the S. flexneri antigens. In conclusion, the results suggest that low calorie intake does not significantly affect the production of milk IgA antibodies to E. coli and S. flexneri antigens in these women. Still, IgM antibodies against certain proteins and LPS molecules of E. coli may be decreased. IgG antibodies, although also present in milk, seemed to be directed mainly against bacterial proteins and not to LPS.
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