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J E Coligan

Publications and source records attributed to J E Coligan.

At least 217 records · Page 12Linked to original sources
PubMed1984

Human T-cell leukemia virus specific antigens.

Type I and type II human T-cell leukemia viruses (HTLV) contain in their genomes three structural genes, gag, pol, and env and a putative transforming gene, lor. Using a living cell membrane immunofluorescence assay, antibodies to surface-expressed env gene products of HTLV-MA have been detected in healthy carriers living in the HTLV-I endemic areas, and in patients with adult T-cell leukemia/lymphoma (ATLL). Similar antibody reactivities were detected in patient MO, from whom HTLV-II was first isolated, and in a proportion of patients with acquired immune deficiency syndrome (AIDS). Amino acid sequence homology between env gene products of HTLV-I and HTLV-II provides the molecular basis for the observed serological crossreactivity. Detection of HTLV-specific antibody in a proportion of AIDS patients suggested that agents related to HTLV-I may be the etiological cause of AIDS. Several lines of evidence have now suggested that HTLV-III is the etiological agent of AIDS. Flanked by the env gene and 3' long terminal repeat (LTR) is a region originally described by Seiki et al. as "X." A 42 kdalton and a 38 kdalton product have been detected in HTLV-I and HTLV-II transformed cells, respectively. These two proteins appear to be translated from a long open reading (lor) frame in the X region, and from a yet to be defined region upstream to the lor gene. The identification of lor products provides direct evidence for the presence of previously unidentified functional genes in HTLV-I and HTLV-II.(ABSTRACT TRUNCATED AT 250 WORDS)

Antigens, Nuclear↗
PubMed1984

Purification and N-terminal amino acid sequence of the human T cell surface antigen T8.

Monoclonal antibodies allow for the detection of structures on the cell surface of human cytotoxic T lymphocytes (CTL) that are involved in their effector function. Among these cell surface components, T8 is of particular interest because it is required during the recognition of target cells by a subset of CTL. An understanding of its role during CTL:target adhesion requires detailed biochemical structural analysis of the T8 molecule. This has been hindered by the small amounts of protein currently available. Here we describe the development of a purification scheme that will permit the accumulation of larger quantities of T8. We studied the binding of T8 to several lectins and determined that one of these, wheat germ agglutinin, bound T8 quantitatively. Experiments designed to test the properties of T8 in a phase separation system with the use of Triton X-114 were performed. These indicated that T8 partitions into the aqueous phase rather than the detergent phase during this procedure. With this in mind, we developed a protocol that resulted in a significant purification of T8 after affinity chromatography. Upon preparative SDS-PAGE followed by electroelution, the T8 antigen was purified to homogeneity and used for N-terminal acid acid sequencing. This analysis yielded the amino terminal 22 amino acids of T8. On purification, it was observed that the protein existed as two bands of Mr 33 and 34 kilodaltons after SDS-PAGE analysis. The relationship between these chains was investigated by limited radio-sequencing and tryptic peptide map analysis; our results indicated that the two polypeptides were identical. The two chains were treated with trifluoromethane sulfonic acid to determine whether carbohydrates accounted for the difference in m.w. This reagent, which cleaves both N-linked and O-linked sugars, cleaved approximately 2000 daltons of oligosaccharides from the T8 molecule. These oligosaccharides are most likely of the O-linked rather than the N-linked variety.

Amino Acid Sequence↗
PubMed1984

Chemical and serologic definition of two unique D region-encoded molecules in the wild-derived mouse strain B10.GAA37.

Detailed serologic and biochemical characterization of D region products of the wild-derived mouse strain B10.GAA37 (Dw16) were performed and compared with previous studies of the D region products of the H-2d,b, and q haplotypes. Serologic analysis revealed that the antigens encoded by the Dw16 region express a unique combination of specificities defined by monoclonal antibodies (mAb) with established activity for the Ld and Dd molecules. Two out of five anti-Ld-reactive mAb reacted with B10.GAA37 cells, whereas one of three anti-Dd mAb showed B10.GAA37 reactivity. Sequential immunoprecipitation of B10.GAA37 antigens demonstrated the existence of at least two antigenically distinct molecules (designated Dw16 and Lw16) encoded by genes associated with the Dw16 region. Peptide map comparisons of the Dw16 and Lw16 molecules defined multiple differences in their primary protein structure, suggesting they are products of separate genes. Structural comparisons of the Lw16 and Dw16 molecules with the Ld and Dd molecules implied a) that the Dw16 and Dd regions did not result from a recent evolutionary divergence of a common primordial haplotype, and b) that the Lw16 and Dw16 molecules are more structurally homologous to each other than the Ld and Dd molecules are. Comparison of these findings with our previous studies of antigens encoded by the D regions suggest that each of these haplotypes has unique properties in terms of the number of gene products expressed and/or the structural relatedness of products of the same region.

Animal Population Groups↗
PubMed1983

A novel HLA-D/DR-like antigen specific for human B lymphoid cells. Biochemical evidence for similarity to but nonidentity with known HLA-D/DR antigens.

The polymorphic human B cell-specific antigen, 33.1, detected by a murine monoclonal antibody, was compared by genetics and structural analysis with known human Ia antigens from a panel of DR homozygous Epstein-Barr virus-transformed B lymphoblastoid cell lines. Cells homozygous for DR 1, 2, 4, 5, and w6 were positive, while cells that are DR3,3 or DR7,7 usually failed to express this antigen. Mutant DR null, DC/MB-positive cells were 33.1 positive while DR null, DC/MB-negative cells failed to express this antigen, suggesting the segregation of 33.1 with the DC antigen. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that 33.1 alpha and beta chains were of lower molecular weights than the DR alpha and beta chains isolated from the same cell line. Partial N-terminal amino acid sequence analyses were carried out for the heavy and light chains of the 33.1 antigen radiolabeled with [3H] phenylalanine. The results of these analyses, in conjunction with previous data on tissue distribution, indicate that the 33.1 antigen is a non-DR but Ia-like antigen closely related to the previously defined I-A homologues, DC and DS.

Amino Acid Sequence↗
PubMed1983

Amino acid sequence of the cytoplasmic segment of the h-2Kd (H2.31) murine major histocompatibility antigen.

The primary structure of the carboxy-terminal portion of the H-2Kd murine major histocompatibility antigen has been determined using radiosequencing methodology. The two peptides encompassing the entire cytoplasmic portion of the H-2Kd molecule were isolated from cyanogen bromide digests of the detergent solubilized molecule. These two peptides are not present in CNBr digests of papain-solubilized H-2Kd. Alignment of the two CNBr peptides was deduced from tryptic overlap peptides derived from the whole molecule. Alignment with the corresponding region of the H-2Kb antigen shows 90% homology and supports the assignment of this segment of H-2Kd as the C-terminal. The sequence obtained in this study is (Met)-Arg-Arg-Asn-Thr-Gly-Gly-Lys-Gly-Val-Asn-Tyr-Ala-Leu-Ala-Pro-Gly-Ser-Gln- Thr-Ser-Asp-Leu-Ser-Leu-Pro-Asp-Pro-Lys-Val-Met-Val-His-Asp-Pro-His-Ser-Leu- Ala. These data allow extensive comparisons with the protein sequences deduced from the 3' ends of H-2d haplotype cDNA and genomic clones as well as with the homologous regions of H-2Kb and H-2Db.

Amino Acid Sequence↗
PubMed1982

Intragenic recombination in an E beta gene for a murine Ia antigen.

The recombinant strain D2.GD was originally typed as I-Ad by serological methods. Indeed, the A alpha and A beta chains of the I-A antigens appear to exhibit normal behavior by the criteria of serology and two dimensional gel analysis. However, the E beta chain encoded by the I-A subregion of this strain, one of the two components of the plasma membrane located I-E antigens produced in D2.GD X A.TFR5)F1 animals, has been demonstrated to be the product of an intragenic recombinational event between E beta genes from the d and b haplotypes. Sequence analysis suggests that the amino-terminal portion of the Eg2 beta chain is derived from the d haplotype and, therefore, that the coding strand for this gene is oriented centromeric leads to telomeric (5' to 3' direction). Finally, these data combined with the data of Rose and Cullen (17) allow the ordering of the genes within the I-A subregion as (H-2K), A alpha, A beta, E beta ... (H-2D).

Amino Acid Sequence↗
PubMed1982

Primary structure of the H-2Db alloantigen. II. Additional amino acid sequence information, localization of a third site of glycosylation and evidence for K and D region specific sequences.

The complete amino acid sequence of the CNBr fragment comprising residues 229-284 of the murine major histocompatibility complex antigen H-2Db has been determined using radiochemical methodology. The sequence was determined by N-terminal sequence analysis of the intact CNBr fragment and by sequence determinations of peptides derived from this fragment by trypsin and staphylococcal V8 protease cleavage. In addition to the amino acid assignments for H-2Db, it was possible to assign the linkage position of the third N-linked glycosyl unit to the asparagine at residue 256. Additional amino acid sequence assignments have also been made for three other CNBr fragments that span residues 99-138, 139-228, and 308-331 of the H-2Db molecule. The total protein sequence information available (222 of 338 residues) agrees in every comparable position with the protein sequence derived from the cDNA clone (pH203) isolated by Reyes and co-workers (1982b), which strongly suggests that this clone encodes H-2Db. Combination of the protein sequence with that deduced from the cDNA clone provides the complete H-2Db protein sequence. Comparison of this sequence with other available protein sequence information for murine class I molecules has revealed protein sequences that may be unique to either K or D region molecules.

Amino Acid Sequence↗
PubMed1982

Rabbit MHC antigens: occurrence of non-beta-2-microglobulin-associated class I molecules.

Two monoclonal antibodies, L12/36 and L13/112, prepared from spleens of BALB/c mice immunized with extracts of the rabbit lymphoid cell line RL-5, precipitate a 42,000 mol. wt molecule from detergent lysates of this cell line. This molecule is not associated with beta-2-microglobulin (beta 2m) and has been shown by sequential precipitation experiments to be antigenically distinct from the population of class I rabbit MHC (RLA) molecules that is associated with beta 2m. In spite of this antigenic difference, amino acid sequence analyses indicate that the RLA heavy chain precipitated with anti-beta 2m and that precipitated with the monoclonal antibodies, have identical N-terminal sequences. The sequence determined to position 36 is GSHSMRYFYTSVSRPGLGXPRFIIVGYVXXTXFVRF. The isoleucine assigned to position 24 is the first species-specific residue found for RLA class I molecules. Analysis of the beta 2m associated and non-associated molecules by two-dimensional gel electrophoresis revealed no differences between the RLA heavy chains. Differences in the subcellular locations of the determinants were indicated by fluorescence microscopy and confirmed by immunoelectron microscopy. It was shown that the specificity recognized by the monoclonal antibodies is principally located on the cytoplasmic face of the plasma membrane whereas the majority of anti-beta 2m reactive specificities are on the extracellular side of the cell membrane.

Amino Acid Sequence↗
PubMed1981

Isolation and sequence analysis of the intramembranous hydrophobic segment of the H-2Kb murine histocompatibility antigen.

The primary structure of the intramembranous segment (TC-1) of the mouse transplantation antigen, H-2Kb, has been determined. The segment contains a stretch of 31 uncharged amino acid residues and is localized between the NH2-terminal and the COOH-terminal hydrophilic regions of the molecule. The amino acid sequence of TC-1 is Trp-Asp-Glu-Pro-Pro-Ser-Thr-Val-Ser-Asn-Met-Ala-Thr-Val-Ala-Val-Leu-Val-Val-Leu -Gly-Ala-Ala-Ile-Val-Thr-Gly-Ala-Val-Val-Ala-Phe-Val-Met-Lys-Met-Arg-(Arg)-(Arg ).

Amino Acid Sequence↗
PubMed1981

Amino acid sequence of the carboxyl-terminal hydrophilic region of the H-2Kb MHC alloantigen. Completion of the entire primary structure of the H-2Kb molecule.

The amino acid sequence of the COOH-terminal hydrophilic region of the H-2Kb histocompatibility antigen was determined. The sequence was completed by analyses of four CNBr fragments obtained from the intact molecule as well as tryptic peptides. This region was composed of 39 amino acid residues with a cluster of basic residues at the NH2 terminus and localized positions 308-346 of the H-2Kb molecule. These sequence data, together with those reported for the NH2-terminal 284 residues [Martinko, J. M., Uehara, H., Ewenstein, B. M., Kindt, T. J., Coligan, J. E., & Nathenson, S. G. (1980) Biochemistry 19, 6188-6193] and for the intramembranous segment [Uehara, H., Coligan, J. E., & Nathenson, S. G. (1981) Biochemistry (preceding paper in this issue)], provided the complete primary structure of the H-2Kb molecule. This is the first histocompatibility antigen for which the entire primary structure is determined.

Amino Acid Sequence↗
PubMed1981

Amino acid sequence of cyanogen bromide fragment CN-C (residues 24-98) of the mouse histocompatibility antigen H-2Dd. A comparison of the amino-terminal 100 residues of H-2Dd, Dd, Kd, and Kb reveals discrete areas of diversity.

The amino acid sequence of the cyanogen bromide (CNBr) fragment extending from position 24 to position 98 of the H-2Dd murine histocompatibility antigen has been determined by using radiochemical microsequencing techniques. This 75-residue fragment (CN-C) is one of two glycopeptides generated by CNBr cleavage of the extracellular portion of the H-2Dd molecule (H-2Dd papain). Determination of this sequence completes the amino-terminal 100 residues of the H-2Dd molecule. The primary structure of CN-C was established by thrombin digestion of isolated CN-C and sequence determination of the three resulting peptides. The COOH-terminal met and its adjacent residue were determined by sequence analysis of a tryptic peptide which overlaps CNBr fragments C and b4 (residues 99-138). Alignment of the thrombic peptides was accomplished by NH2-terminal sequence analyses of CN-C and peptides generated by Staphylococcus aureus V8 protease digestion of CN-C. The sequence data presented here, together with that already given for H-2Dd [Nairn, R., Nathenson, S. G., & Coligan, J.E. (1980) Eur. J. Immunol. 10,495-503], allow a comparison of the NH2-terminal 100 residues of the Dd, Db, Kd, and Kb molecules. Discrete areas of diversity, in particular, one between residues 62 and 83, are obvious. Comparison over some 180 residues of the Dd and Kb molecules reveals a particularly close similarity between these products of a K and a D gene from widely disparate mouse strains.

Amino Acid Sequence↗