Two glycosylation alterations of mouse intestinal mucins due to infection caused by the parasite Nippostrongylus brasiliensis

被引:34
作者
Holmén, JM [1 ]
Olson, FJ [1 ]
Karlsson, H [1 ]
Hansson, GC [1 ]
机构
[1] Gothenburg Univ, Dept Med Biochem, SE-40530 Gothenburg, Sweden
关键词
mucin; O-glycosylation; oligosaccharides; parasite infection; fucosyltransferase;
D O I
10.1023/A:1022589015687
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The glycosylation alterations of mouse small intestinal mucins during a 12-day infectious cycle caused by the parasite Nippostrongylus brasiliensis have been studied. The guanidinium chloride insoluble mucins were isolated at day 0 to 12 from the small intestine of infected and non-infected C57BL/6 mice. The O-linked oligosaccharides were released by reductive beta-elimination from the mucins and separated into neutral, sialylated and sulfated fractions. All fractions were analyzed by monosaccharide composition analysis and the neutral oligosaccharides were structurally characterized by gas chromatography/mass spectrometry. Two oligosaccharides containing blood group H-type epitopes (Fucalpha1-2Gal-) were transiently expressed with a maximum at day 6. Additional oligosaccharides with the common structure HexNAcGal-3GalNAcol were transiently induced with a maximum at day 10. Northern blot analysis on total RNA showed a transient expression at day 4-6 of the Fut2 gene encoding a Fucalpha1-2 fucosyltransferase, probably responsible for the detected blood group H-type epitopes. Comparisons with the corresponding infection in rat studied previously, revealed structurally different alterations, although occurring as transient events in both species. Both showed an induced blood group-type transferase halfway through the infection (a blood group A transferase in rat) and an induced transferase adding a terminal GalNAc (to a sialic acid-containing epitope in rat) towards the end of the infection. These differences between closely related species suggest rapid evolutionary alterations in glycosyltransferase expression.
引用
收藏
页码:67 / 75
页数:9
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