ORCID Profile
0000-0002-7192-0109
Current Organisation
University of Veterinary Medicine Vienna
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Publisher: Elsevier BV
Date: 04-2014
DOI: 10.1016/J.JPROT.2014.02.018
Abstract: Haptoglobin (Hp) and immunoglobulins are plasma glycoproteins involved in the immune reaction of the organism after infection and/or inflammation. Porcine circovirus type 2-systemic disease (PCV2-SD), formerly known as postweaning multisystemic wasting syndrome (PMWS), is a globally spread pig disease of great economic impact. PCV2-SD affects the immunological system of pigs causing immunosuppression. The aim of this work was to characterize the Hp protein species of healthy and PCV2-SD affected pigs, as well as the protein backbone and the glycan chain composition of porcine Hp. PCV2-SD affected pigs had an increased overall Hp level, but it did not affect the ratio between Hp species. Glycoproteomic analysis of the Hp β subunits confirmed that porcine Hp is N-glycosylated and, unexpectedly, O-glycosylated, a PTM that is not found on Hp from healthy humans. The glyco-profile of porcine IgG and IgA heavy chains was also characterized decreased levels of both proteins were found in the investigated group of PCV2-SD affected pigs. Obtained results indicate that no significant changes in the N- and O-glycosylation patterns of these major porcine plasma glycoproteins were detectable between healthy and PCV2-SD affected animals. PCV2-SD is a disease of great economic importance for pig production, characterized by a complex response of the immune system. In the search of a better diagnostic rognostic marker for porcine PCV2-SD, extensive analyses of the Hp protein backbone and the glycan chains were thoroughly analyzed by various techniques. This resulted in detection and confirmation of Hp O-glycosylation and the glyco-profiling of porcine IgG and IgA. The N- and O-glycosylation of these major porcine plasma glycoproteins appears to be not affected by PCV2-SD infection. Interestingly, these data suggest that this viral infection, which significantly affects the immune responses of the host, leaves the biosynthetic glycosylation processes in the liver and immune cells unaffected. Lack of PTM changes is in contrast to findings in humans where for both proteins pattern changes have been reported in several chronic and inflammatory diseases. This underlines the importance of studying species in detail and not reaching to conclusions by analogy. Furthermore, since Hp is usually quantified by immunoassays in clinical routine analyses, our findings indicate that no bias in Hp determination capabilities due to an altered carbohydrate pattern is to be expected.
Publisher: Wiley
Date: 1999
DOI: 10.1002/(SICI)1522-2683(19990101)20:4/5<836::AID-ELPS836>3.0.CO;2-6
Publisher: Elsevier BV
Date: 2017
Publisher: Wiley
Date: 12-1999
DOI: 10.1002/(SICI)1522-2683(19991201)20:18<3599::AID-ELPS3599>3.0.CO;2-K
Publisher: Wiley
Date: 25-11-1999
Publisher: Springer Science and Business Media LLC
Date: 06-12-2016
DOI: 10.1038/SREP38378
Abstract: Major urinary proteins (MUPs) are often suggested to be highly polymorphic, and thereby provide unique chemical signatures used for in idual and genetic kin recognition however, studies on MUP variability have been lacking. We surveyed populations of wild house mice ( Mus musculus musculus ), and examined variation of MUP genes and proteins. We sequenced several Mup genes (9 to 11 loci) and unexpectedly found no inter-in idual variation. We also found that microsatellite markers inside the MUP cluster show remarkably low levels of allelic ersity, and significantly lower than the ersity of markers flanking the cluster or other markers in the genome. We found low in idual variation in the number and types of MUP proteins using a shotgun proteomic approach, even among mice with variable MUP electrophoretic profiles. We identified gel bands and spots using high-resolution mass spectrometry and discovered that gel-based methods do not separate MUP proteins, and therefore do not provide measures of MUP ersity, as generally assumed. The low ersity and high homology of Mup genes are likely maintained by purifying selection and gene conversion, and our results indicate that the type of selection on MUPs and their adaptive functions need to be re-evaluated.
No related grants have been discovered for Ingrid Miller.