Human T Cell Antigen Expression by Primate T Cells

Haynes, BF; Dowell, DL; Hensley, Lisa E.; Gore, Ira; Metzgar, RS

doi:10.1126/science.6171885

Cited by 106 publications

(40 citation statements)

References 16 publications

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“…Previous reports had claimed that the CD4/CD8 ratio in macaques was inverted (2,3,22) and these findings raised concerns about similarities between immune systems in these species. When CD4/CD8 ratios were calculated using CD8 T-cell counts defined by the CD8ϩ alone, our values were around the value of 0.75-1.3.…”

Section: Discussionmentioning

confidence: 82%

Importance of the CD3 marker for evaluating changes in rhesus macaque CD4/CD8 T-cell ratios

Dykhuizen¹,

Ceman²,

Mitchen³

et al. 2000

Cytometry

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Section: Discussionmentioning

confidence: 82%

Importance of the CD3 marker for evaluating changes in rhesus macaque CD4/CD8 T-cell ratios

Dykhuizen¹,

Ceman²,

Mitchen³

et al. 2000

Cytometry

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“…Given that T11 is more phylogenetically conserved than any known human T-lineage structure (12), appears earliest during intrathymic ontogeny, and, unlike the Ti a and ,B subunits (13), is monomorphic, thus containing no variable domains, it is possible that T11 represents a primitive T-cell surface activation molecule. Primary sequence information might suggest a mechanism by which T11 mediates signal transduction.…”

mentioning

confidence: 99%

Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes.

Sayre¹,

Chang²,

Hussey³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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The T11 (CD2) sheep-erythrocyte-binding protein is a T-cell surface molecule involved in activation of T lymphocytes and thymocytes, including those lacking the T3-Ti antigen-receptor complex. The primary structure of Til was deduced from protein microsequencing and cDNA cloning. The mature human protein appears to be divided into three domains: a hydrophilic 185 amino acid external domain bearing only limited homology to the T-cell surface protein T4 and the immunoglobulin K light chain variable region, a 25 amino acid hydrophobic transmembrane segment, and a 126 amino acid cytoplasmic domain rich in prolines and basic residues. Transfection of cDNAs encoding either the 1.7-or the 1.3-kilobase Til mRNA into COS-1 cells resulted in expression of surface Til epitopes as well as sheep-erythrocyte-binding capacity. The predicted structure is consistent with the possibility that Til functions in signal transduction.Human thymus-derived (T) lymphocytes were originally distinguished from B lymphocytes and other hematopoietic cells by their ability to form spontaneous aggregates (E rosettes) with sheep erythrocytes (SRBCs) (1-3). Congenital hypoplasia of the thymus results in loss or significant diminution of peripheral blood E-rosette-forming cells, thus attesting to the importance of the thymus in the maturation of lymphocytes bearing surface receptors for SRBCs.The structure mediating the SRBC binding property is a 50-kDa single-chain cell surface protein (4)(5)(6)(7)(8). Three distinct surface epitopes termed T111, T112, and T113 can be defined. Whereas the T111 and T112 epitopes are expressed on both resting and activated T cells, T113 is spatially distinct and preferentially expressed after T-lineage activation. The SRBC binding site on T11 appears to be identical or closely associated with the T111 epitope, because antibodies to T111 but not T112 or T113 block the ability of SRBCs to form rosettes with T lymphocytes (8). Perhaps more important, antibodies to the T111 epitope also broadly inhibit T-cell responses. In contrast, a combination of anti-T112 plus anti-T113 induces interleukin 1 (IL-1)-independent polyclonal T-cell activation. Thus, interaction of monoclonal antibodies with the T11 structure produces either profound agonistic or antagonistic effects on T-cell activation.Stimulation of T cells through T11, like that occurring through the T3-Ti antigen/MHC receptor complex (which recognizes antigen in the context of major histocompatibility complex-encoded proteins), is mediated via an interleukin 2 (IL-2)-dependent pathway involving activation of endogenous IL-2 and IL-2-receptor genes (8). Nevertheless, these surface structures are not physically linked to one another, since (i) immunoprecipitation and comodulation studies fail to demonstrate any association between T11 and individual T3-Ti subunits (9) and (ii) the T11 pathway functions in early thymocytes and natural killer cells, both of which lack the surface T3-Ti complex (10, 11).Given that T11 is more phylogenetically conserved than any ...

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“…Most antibodies of the same type showed similar reactivity, but a few of them varied in reactivity with the panel cells. We did not examine cell lines of gorillas and orangutans, but the epitope defined by H-45 appeared to be human-specific, because H-45 did not react with a T-cell line of a chimpanzee, which is known to express T-cell antigens that cross-react with those of humans (8). With these panel cell lines, the reactivity of antibodies H-Cl and H-44 of the H-31-type and H-45 of the HIEI-type was different from that of other H-31-type and HIEI-type antibodies, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, well-defined monoclonal antibodies to human major histocompatibility antigens (4) and human T-cell markers (8) have also been used for phylogenetic studies on primates. Haynes et al (8) showed that the antigenic determinants of the SRBC-receptor, but not the determinants of the other T-cell subset marker molecules, have been highly conserved during primate evolution, and that human, gorilla, and chimpanzee T cells have identical reactivity with the monoclonal antibodies to human T-cell subset antigens.…”

mentioning

confidence: 99%

New Monoclonal Antibodies That Define Multiple Epitopes and a Human‐Specific Marker on the Interleukin 2 Receptor Molecules of Primates

Tanaka

Inoi

Tozawa

et al. 1986

Microbiology and Immunology

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Twelve hybridoma cell lines producing monoclonal antibodies to the human interleukin 2 (IL-2) receptor (IL-2R) molecule were prepared. These antibodies were characterized by competitive antibody-binding assay and sequential immunoprecipitation assay with four known monoclonal antibodies to the human IL-2R molecule. The twelve new monoclonal antibodies were divided among the four known antibody types, the HIEI-, H-A26-, H-31-, and anti-Tac-type, and an additional new type, the H-48-type. The H-48 antibody did not compete with any other antibodies in the competitive binding assay. The binding of 1-25I-IL-2 to MT-2 cells and the IL-2-dependent growth of normal activated T-cells were both strongly inhibited by all the H-31-and anti-Tac-type antibodies, and partially or slightly inhibited by HIEI-and H-A26-type antibodies, but were not inhibited by the H-48 antibody. Thus, the same type of monoclonal antibodies had a similar effect on the function of IL-2R. These results suggest that epitopes for the same type of antibodies could be single identical epitopes or epitopes closely associated with each other. On the other hand, these antibodies also reacted variously with a panel of various human and simian lymphoid cell lines immortalized with human T-cell leukemia virus type-I (HTLV-I) : the H-45 antibody reacted only with the human cell lines, the H-Cl and H-44 and H-47 antibodies reacted with human and ape cell lines, and the other antibodies reacted with cell lines of humans, apes and Old and New World monkeys. These differences in the reactivity of the antibodies with the primate cell lines suggest that the antigenic structure of the IL-2R molecule changed during evolutionary divergence of the primates.

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Human T Cell Antigen Expression by Primate T Cells

Cited by 106 publications

References 16 publications

Importance of the CD3 marker for evaluating changes in rhesus macaque CD4/CD8 T-cell ratios

Importance of the CD3 marker for evaluating changes in rhesus macaque CD4/CD8 T-cell ratios

Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes.

New Monoclonal Antibodies That Define Multiple Epitopes and a Human‐Specific Marker on the Interleukin 2 Receptor Molecules of Primates

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