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J Hasler-Rapacz

Publications and source records attributed to J Hasler-Rapacz.

25 records · Page 2Linked to original sources
PubMed1986

Polymorphism and inheritance of swine small intestinal receptors mediating adhesion of three serological variants of Escherichia coli-producing K88 pilus antigen.

Brush borders, enterocytes, or both preparations obtained from the small intestine of 345 pedigreed pigs, carrying components of seven breeds, were tested by adhesion assay in vitro with 6-32 enteropathogenic Escherichia coli strains, each expressing one of the three K88 pilus antigens, K88ab, K88ac and K88ad. With few exceptions, all pigs were classified as belonging to one of four adhesion phenotypes: I I--corresponding to K88ab(-),ac(-),ad(-); II--K88ab(-),ac(-),ad(+); III--K88ab(+),ac(+),ad(-); and IV--K88ab(+),ac(+),ad(+). The non-adhering phenotype I was found to be the most frequent among the pigs tested, with the exception of one commercial herd, and this phenotype seems to be inherited as a recessive trait. The remaining three phenotypes are adhering, or are susceptible to adherence by one K88 variant, K88ad (phenotype II), by two variants, K88ab, ac (phenotype III), or by all three K88 variants, K88ab,ac,ad (phenotype IV). Phenotype II was found to be at low frequency, whereas III and IV occurred with similar frequencies. While the prevailing phenomenon was the bacterial adhesion to all, or none, of the brush borders, some pigs exhibited both adhering and non-adhering brush borders, a mixed adherence phenotype. Preliminary segregation data, obtained from the F1 generation, seem to indicate that phenotypes III and IV correspond to two haplotypes with genes at two or three closely linked loci respectively. An alternative hypothesis is that the phenotypes III and IV are expressions of alleles at a single locus, each allele specifying a receptor able to bind two or three different serological types of K88 E. coli.

Animals↗
PubMed1986

Linkage between the porcine genes encoding immunoglobulin heavy-chain allotypes and some serum alpha-protease inhibitors: a conserved linkage in pig, mouse and human.

Linkage between the genes coding for immunoglobulin heavy-chain allotypes and some serum alpha-protease inhibitors was demonstrated in pigs by means of segregation data in families. A recombination frequency of about 8% was estimated. This represents evolutionary conservation of an autosomal linkage group as linkage between the homologous loci has previously been reported, in humans and in mice.

Animals↗
PubMed1982

Lipoprotein immunogenetics in primates. I. Two serum beta-lipoprotein allotypes (Lmb1 and Lmb11) in rhesus monkeys and the LP-B immunological relationship with other primates.

Immunogenetic investigations on two serum beta-lipoprotein allotypes of rhesus monkeys (Macaca mulatta) are reported. The allotypes, designated Lmb1 and Lmb11, are associated with the main lipoprotein family, LP-B or beta-lipoprotein, expressed on independent beta-molecules, and classify rhesus monkeys into three phenotypes: Lmb1, Lmb11, and Lmb1,11. Genetic and molecular studies indicate that the allotypes are encoded by two codominant autosomal allelic genes, Lmb1 and Lmb11. Anti-Lmb1 cross-reacts with the sera of two other macaque species, whereas anti-Lmb11 with sera of all Old World monkeys. Heteroimmune sera, antihuman apo-B and antirhesus LP-B, showed high but diversified degrees of cross reactivity with other primates.

Animals↗
PubMed1981

Immunogenetic studies on low-density lipoprotein allotypes in chickens (Lcp1 and Lcp2).

Two blood plasma lipoprotein allotypes are described. Specific antiallotypic reagents were obtained from alloimmune precipitating sera produced against normal plasma and subsequently against lipoprotein fraction of d less than 1.072 g/ml. Identification studies by means of centrifugation and specific staining show that Lcp1 and Lcp2 are markers of the low-density lipoprotein class, 1.006 less than d less than 1.063 g/ml. Serological and genetic studies indicate that the two alloantigens behave as products of allelic genes, each occurring with varying frequencies in 20 lines studies. The Lcp1 antigen is always accompanied by Lcp2; however, the latter was also found to occur in plasma of birds lacking the Lcp1 marker.

Animals↗
PubMed1976

Immunogenetic polymorphism of lipoproteins in swine. 1. Four additional serum beta-lipoprotein allotypes (Lpp2, Lpp4, Lpp5 and Lpp15) in the Lpp system.

Four additional swine serum lipoprotein allotypes are described. Specific anti-allotype reagents were obtained from alloimmune precipitating sera produced in lipoprotein-defined-type recipients immunized with normal sera and subsequently with lipoprotein fractions. Identification studies indicate that the four serologically defined low-density lipoprotein (LDL) variants, designated Lpp2, Lpp4, Lpp5 and Lpp15, are members of a previously described Lpp system. The individual specificities, Lpp2, Lpp4 and Lpp5, are determined by three co-dominant autosomal genes, Lpp2, Lpp4 and Lpp5, respectively, whereas the common specificity, Lpp15, is controlled by a complex of genetic information of the Lpp2 and Lpp4 genes, and by the two previously described alleles, Lpp1 and Lpp3; Lpp15 occurs on the same molecule with respective individual specificity. The Lpp5 and Lpp15 antigens behave as a pair of alternative allotypic specificities. The double immunodiffusion test in agar was employed to demonstrate independent phenotypic expression of each allelic gene in the Lpp heterozygous animals, for the analysis of the immune sera, and for lipoprotein testing of 3305 sera. Marked differences in gene frequencies were found between the swine breeds tested. As a result of characteristic frequencies, only nine of 15 possible Lpp genotypes were found in the breeding herds tested; the remaining six genotypes were obtained from testcross matings.

Alleles↗
PubMedDate not supplied

Studies in swine on inheritance and variation in expression of small intestinal receptors mediating adhesion of the K88 enteropathogenic Escherichia coli variants.

Small intestinal enterocyte preparations from 368 pigs were phenotyped by an in vitro adhesion test using six strains of K88 Escherichia (E.) coli, each expressing one of three K88 fimbrial antigenic variants: K88ab, K88ac, or K88ad. All pigs tested were classified into one of four adhesion brush border phenotypes: I (K88ab-, K88ac-, K88ad-); II (K88ab-, K88ac-, K88ad+); III (K88ab+, K88ac+, K88ad-); or IV (K88ab+, K88ac+, K88ad+). The segregation and adhesion affinity data suggest that there are two adhesion affinity receptors for K88ad+ E. coli: a high affinity (adH) and a low affinity (adL) receptor. The high affinity receptor cosegregates with receptors for K88ab and K88ac fimbrial antigens forming together the phenotype IV; the low affinity receptor is associated with the adhesion phenotype II, and its physiological expression is terminated by 16 weeks of age. In contrast, the K88adH receptor is expressed during the entire life cycle. The presence of a mixed adhesion phenotype, K88adM, assumed to be determined by K88ab(-),ac(-),adL(+)/K88ab(+),ac(+),adH(+) heterozygous genotype, is interpreted as an indication that each of the two types of brush border adhesion for the K88ad antigen is expressed on independent enterocytes.

Aging↗