Biomedical subjects

S E Stroup

Publications and source records attributed to S E Stroup.

3 recordsLinked to original sources

PubMed2000

The ves multigene family of B. bovis encodes components of rapid antigenic variation at the infected erythrocyte surface.

B. bovis, an intraerythrocytic protozoal parasite, establishes chronic infections in cattle in part through rapid variation of the polymorphic, heterodimeric VESA1 protein on the infected erythrocyte surface and sequestration of mature parasites. We describe the characterization of the ves1 alpha gene encoding the VESA1a subunit, thus providing a description of a gene whose product is involved in rapid antigenic variation in a babesial parasite. This three-exon gene, a member of a multigene family (ves), encodes a polypeptide with no cleavable signal sequence, a single predicted transmembrane segment, and a cysteine/lysine-rich domain. Variation appears to involve creation and modification or loss of a novel, transcribed copy of the gene.

Amino Acid Sequence↗

PubMed1997

Characterization of a variant erythrocyte surface antigen (VESA1) expressed by Babesia bovis during antigenic variation.

Babesia bovis, an intraerythrocytic, protozoal parasite of cattle, undergoes clonal antigenic variation (Allred DR, Cinque RM, Lane TJ, Ahrens KP. Infect Immun 1994;62:91-98). This ability could provide a mechanism by which the parasite escapes host immune defenses to establish chronic infection. Previous work identified two parasite-derived antigens of Mr 128,000 and 113,000 that were present on the surface of the infected erythrocyte and appeared to be associated with clonal antigenic variation (Allred DR, Cinque RM, Lane TJ, Ahrens KP. Infect Immun 1994;62:91 98). Two monoclonal antibodies (mAbs), 3F7.1H11 and 4D9.1G1, which recognize the variant erythrocyte surface antigen (VESA1) have been identified. These mAbs react only with the surface of erythrocytes infected with the B. bovis C9.1 clone in live-cell immunofluorescence assays. In both conventional and surface immunoprecipitations, the mAbs precipitate a variant antigen doublet that matches in mass the infected red blood cell (IRBC) surface antigens precipitated with bovine serum. In contrast, Western blot analysis revealed that only the Mr 128,000 polypeptide is recognized by the mAbs. Neither mAb recognizes antigenically variant progenitor or progeny parasite clones in any of the immunoassays, confirming the involvement of this antigen in rapid clonal antigenic variation. Failure to label this antigen with [9,10(n)-3H]myristic acid, [9,10(n)-3H]palmitic acid or D-[6-3H]glucosamine indicates that these polypeptides are neither N-glycosylated nor fatty acylated. Identity of the variant antigen recognized by the mAbs with that putatively identified with immune serum was confirmed by comparison of partial proteolytic digestion products. Unambiguous identification of the VESA1 antigen as a component of antigenic variation will facilitate characterization of the events leading to antigenic variation on the B. bovis-infected erythrocyte surface and its significance to parasite survival during chronic infection.

Acylation↗

PubMed1993

Traumatic root resorption in dentine-immunized mice.

Traumatic root resorption in a mouse model has been shown to coincide with a decline in naturally occurring serum antibody levels to dentin. It has been proposed that root resorption may be dentin antibody mediated. The purpose of this study was to examine the traumatic root resorption response in mice after hyperimmunization with a crude tooth extract (dentin). The hypothesis of this study was that elevated dentin antibody titers would positively correlate with root resorption. Mice were immunized with mouse dentin and controls were sham immunized. All mice were boosted 4 weeks later with or without mouse dentin as appropriate. All mice were then boosted two more times at weekly intervals with mouse dentin and then twice at weekly intervals with rat dentin. The change to rat dentin was made to increase mouse serum antibody titers to dentin. Serum samples were obtained before the initial immunization and weekly after each boost and were examined for antibody-to-dentin antigen by the enzyme-linked immune sorbent assay (ELISA). One week after the second boost with rat dentin, all animals were exposed to the cryoprobe procedure. Mice were killed 10 days later, and serum tested for antibody to dentin antigen. The incisors were examined by scanning electron microscopy, and root resorption quantified. Root resorption was observed on the incisors in the sham-immunized mice but not in the dentin-immunized mice. A trend toward increased serum antibody titers to dentin in immunized mice was observed over time.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗