PubMed · 7381813
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D Goode. 1980. A serological test for tuberculosis.. https://doi.org/10.1136/jramc-126-01-05
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The Duffy blood group system is of clinical and biological significance. Antibodies to Duffy antigens are responsible for some cases of transfusion incompatibility and newborn hemolytic disease. The Duffy protein is a receptor for the Plasmodium vivax erythrocyte-binding protein and is also a receptor for various chemokines (thus renamed Duffy Antigen Receptor for Chemokines [DARC]). The two Duffy polymorphic antigens, Fya and Fyb (coded by the FY*A and FY*B alleles), are present on erythrocyte membranes. The Fy(a-b-) phenotype is the predominant one in populations of black people and also occurs in other populations, including some non-Ashkenazi Jewish groups. The Fy(a-b-) phenotype has been associated with a mutation in the FY*B promoter at the GATA box that abolishes the expression of erythrocyte Duffy protein. We describe here a novel mutation, present in the FY*B coding sequence (271C --> T), that is associated with some Fy(b-) phenotypes among non-Ashkenazi Jews and among Brazilian blacks. The mutation is present in Fy(b-) individuals, who have wild-type FY*B GATA and carry the previously described 304G --> A substitution. The 271C --> T and 304G --> A can be identified by restriction enzyme-generated restriction fragment length polymorphisms. The 271C --> T substitution represents a considerable change in chemical nature (Arg91 --> Cys), one which may affect the antigenic determinants of DARC, and thus be of clinical significance. The mutation may have implications for some physiological roles of DARC and be of interest in malaria research and in studies of population genetics.
Epitope specificity and isotype influence mAb efficacy against Cryptococcus neoformans; however, the relative contribution of each attribute is poorly understood. To date, only mAbs that recognize two epitopes of capsular glucuronoxylomannan (GXM), defined by the IgG1 mAbs 2H1 and E1, consistently mediate protection against C. neoformans. The role of epitope specificity was further examined using six additional IgG1 mAbs and serotype D C. neoformans ATCC 24067. mAbs 3C2, 439, and 471 recognize the 2H1 epitope, whereas mAbs 339, 1255, and 302 recognize two separate epitopes. mAbs 3C2, 439, and 471 competed for GXM with the IgA mAb 18G9, a 2H1 mAb family member, whereas mAbs 302, 339, and 1255 did not. Each mAb bound GXM similarly, as determined by agglutination, direct Ag binding, Ag inhibition, and indirect capsular immunofluorescence assays. mAb apparent affinity constants for GXM ranged from 5 to 26 x 10(7) M(-1) with mAb 1255 > 3C2 > 339 > 439 > 471 > 302. Each mAb significantly prolonged survival (p < 0.05); the average survival times of control and mice passively immunized with mAbs 3C2, 302, 339, 439, 471, and 1255 were 10.8, 36.6, 33, 25.5, 24.9, 17, and 22.6 days, respectively. Although each mAb enhanced J774.16 cell fungicidal activity, differences were observed in the ability of each mAb to facilitate attachment and ingestion of cryptococci. These results indicate 1) two additional epitope specificities associated with mAb efficacy, 2) differences in opsonic and protective efficacy for IgG1 anti-GXM mAbs, 3) an association between affinity and protective efficacy, and 4) additional support for association between an annular indirect capsular immunofluorescence pattern and mAb efficacy.
The biological characteristics of isolates of T. evansi collected from buffalo in different provinces in North Vietnam was determined in terms of their sensitivity to drugs currently used in the treatment of trypanosomosis. Five isolates were collected from buffalo, cloned and then tested against Trypamidium, Samorine, Naganol and Veriben. All isolates were sensitive to Naganol and Veriben. An isolate from a buffalo in Ha bac province (Hb1) was the least sensitive with trypamidium at a CD80 > 128 mg/kg, more than 8 times the CD 100 of the remaining isolates (16 mg/kg). An antigen-detection enzyme immunoassay (Ag-ELISA) based on a T. evansi-specific monoclonal antibody was evaluated for its ability to detect infections with T. evansi in buffalo. The sensitivity of the Ag-ELISA was 63% and the specificity 75%. The positive predictive value of this assay was too low to allow identification of individual infected animals on the results of a single test in the districts investigated. For definitive diagnosis, a serial testing protocol was used, where a more specific test, the card agglutination test (CATT) was used initially and any positive samples was then checked by the Ag-ELISA.