PubMed · 4549534
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O Prokop, N Nenkov, A Rackwitz. 1974. [Studies on the problem "Sid" and "Cad"].. https://pubmed.ncbi.nlm.nih.gov/4549534/
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A protein isolated and purified from extracts of bark strips from mature rubber (Hevea brasilinsis) agglutinated erythrocytes from rabbits and all human blood types except AB. No agglutination was detected with erythrocytes from sheep, rates or mice. Proteolytic treatment of Hevea bark lectin (HBL) abolished haemagglutinin activity. The M(r) determined by SDS-PAGE was 40 k and that estimated from gel filtration was 140 k. Fetuin, asialofetuin, bovine submaxillary mucin and asialosubmaxillary mucin inhibited HBL-induced agglutination of rabbit erythrocytes. The HBL showed maximum haemagglutination activity over the pH range 4.5-9.5 and heat stability up to 60 degrees.
We have examined the immunohistochemical distribution of H Type 1 and of H Type 2 substances of the ABO blood group system in human submandibular gland using either of the two anti-H monoclonal antibodies MAb 1E3 and MAb 3A5. MAb 3A5 was specific for H Type 2, and MAb 1E3 reacted with each of H Type 1-H Type 4 artificial antigens. We have developed a competitive inhibition method against H Type 2 and have obtained MAb 1E3, which is fairly specific for H Type 1 under certain conditions. Mucous cells from secretors were strongly stained by 1E3 and weakly by 3A5, whereas those from nonsecretors showed no reaction with 1E3 and 3A5. Serous cells from both secretors and nonsecretors were stained neither by 1E3 nor by 3A5. Striated and interlobular duct cells were strongly stained by 1E3 and by 3A5, regardless of the secretor status. These results indicated that the expressions of the H Type 1 and H Type 2 in different cell types of the submandibular gland were controlled by different genes. In addition, we have determined the acceptor specificity of two alpha(1,2)fucosyltransferases (H and Se enzymes) after transient expressions of the FUT1 and FUT2 in COS7 cells, and found that the H enzyme activity was similar for both Type 1 and Type 2 precursors, and that Se enzyme activity with the Type 1 precursor was higher than that with the Type 2 precursor. Expression of the H Type 1 antigen in mucous cells was found to be dependent on the Se gene, whereas expressions of the H Type 1 and H Type 2 antigens in striated and interlobular duct cells were dependent on the H gene. (J Histochem Cytochem 46:69-76, 1998)
Rotavirus VP8*, the N-terminal trypsin cleavage product of VP4, has been shown to bind to MA-104 cells and human O type erythrocytes. To examine whether bacterially expressed VP8* binds to cellular components of MA-104 cells, the VP8* (aa 1-247) was expressed in E. coli and radiolabelled with 35S-methionine. The radiolabelled rVP8* was immunoprecipitated with antiserum to bovine rotavirus C486 (BRV). The rVP8* was found to bind to MA-104 cells and its binding was competed by BRV. To study the interaction between VP8* and receptors of erythrocytes, hemagglutination (HA) and hemagglutination inhibition (HI) assays were carried out using solubilized rVP8*. rVP8* showed HA which could be inhibited by antiserum to BRV. This interaction was also inhibited by gangliosides, demonstrating a sialic acid dependent interaction. To study the contribution of the C-terminal region of VP8* to HA, a number of approaches were used. First, a peptide spanning aa 230-247 was synthesized and antisera was raised against the peptide to see whether it could inhibit HA of rVP8*. Second, a truncated form of VP8* (tVP8*: aa 1-229) was expressed to examine its hemagglutinating activity. Third, the dimerization of rVP8* and tVP8* was compared by Western-blotting following electrophoresis using native SDS-PAGE. The results indicated that antibody to aa 230-247 inhibits hemagglutination by preventing dimerization of VP8* which in turn allows the molecule to cause HA. To characterize the interaction between the HA domain and sialic acid receptors, erythrocytes were treated with sialidases of different specificities. Arthrobacter ureafaciens, Clostridium perfringens and alpha 2-8 linkage-specific neuraminidase destroyed the ability of sialic acid of erythrocytes to interact with rVP8*, indicating that bovine rotavirus C486 binding requires an alpha 2-8 linkage but acetylation of the sialic acid is not necessary.