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  • 1
    Electronic Resource
    Electronic Resource
    Oligonucleotide-poly(L-lysine)-heparin complexes: Potent sequence-specific inhibitors of HIV-1 infection (1994)
    s.l. : American Chemical Society
    Bioconjugate chemistry 5 (1994), S. 8-13 
    Details
    ISSN: 1520-4812
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bc00025a002
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  • 2
    Electronic Resource
    Electronic Resource
    Synthetic CD4 exocyclics inhibit binding of human immunodeficiency virus type 1 envelope to CD4 and virus replication in T lymphocytes (1997)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 15 (1997), S. 150-154 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] CD4 functions as a major T-cell surface receptor for human immunodeficiency virus by binding the human immunodeficiency virus type 1 (HIV-1) envelope protein gp120 with relatively high affinity. We have developed constrained aromatically modified analogs of the secondary structures of the first ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0297-150
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  • 3
    Electronic Resource
    Electronic Resource
    Direct evidence for chromosomal inversion during T-cell receptor β -gene rearrangements (1986)
    [s.l.] : Nature Publishing Group
    Nature 319 (1986), S. 28-33 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A germline T-cell receptor variable region (Vβ) gene segment (Vβ14) has been mapped 10 kilobases to the 3′ side of the constant region (Cβ2) gene. The Vβ14 gene segment is in an inverted transcriptional polarity relative to the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/319028a0
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  • 4
    Electronic Resource
    Electronic Resource
    A novel complex of proteins binds the HIV-1 promoter upon virus interaction with CD4 (1998)
    Springer
    Journal of biomedical science 5 (1998), S. 281-289 
    Details
    ISSN: 1423-0127
    Keywords: CD4 ; Signaling ; HIV transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract HIV-1Lai13EM is a mutant isolate which is less sensitive than the parental HIV-1Lai strain to an in vitro treatment with 13B8-2 anti-CD4 monoclonal antibody (mAb) that generally inhibits transcription of HIV-1 and HIV-2. In contrast to other clade B viruses, this isolate carries a point mutation G〉A at position −188 of the viral promoter. The fact that HIV-1NDK, a clade D virus insensitive to 13B8-2 mAb, also carries an A nucleotide at this position has brought our attention to the sequence surrounding position −188. Here we analyzed whether a DNA-binding molecule interacts with this region. Electrophoretic mobility shift assays performed with the −201/−175 HIV-1Lai wild-type sequence or the sequence containing a point mutation G〉A at position −188 demonstrated their ability to bind a heterotrimeric complex induced in CEM cells by stimulation with heat-inactivated HIV-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02255860
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  • 5
    Electronic Resource
    Electronic Resource
    Structural and functional properties of HIV-1GER TAR sequences (1996)
    Springer
    Journal of biomedical science 3 (1996), S. 31-40 
    Details
    ISSN: 1423-0127
    Keywords: HIV ; Duplicated sequence ; Transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Sequencing of HIV-1GER long terminal repeat (LTR) has demonstrated, for the first time in an HIV-1 primary isolate, a TAR duplication refered to as TAR1 (nucleotides +1 through +68) and TAR2 (nucleotides +69 through +136). This TAR duplication is stable during replication of HIV-1GER isolate in CEM cells. Analysis of LTR-CAT reporter constructs demonstrated that under Tat transactivation the HIV-1GER/LTR (containing TAR1 and TAR2) was expressed at a higher level than a similar construct (HIV-1GERΔTAR) containing a single TAR sequence. Among the two transcription initiation sites found in the HIV-1GER/LTR, only the most 5′ start site was shown to be functionally active. The predicted secondary structure of the 5′-end mRNAs of HIV-1GER suggests it may fold into a double TAR hairpin which resembles that of HIV-2. Finally, HIV-1GER Tat protein shows primary sequence similarity with Tat proteins from other isolates of HIV-1 and is apparently unrelated to HIV-2 Tat proteins. This work provides the first evidence of a TAR sequence duplication in HIV-1 which increases the efficiency of transactivation by Tat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02253576
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  • 6
    Electronic Resource
    Electronic Resource
    Clonal analysis of B- and T-cell responses to Ia antigens (1981)
    Springer
    Immunogenetics 14 (1981), S. 481-495 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Thirty-five Iak-specific monoclonal alloantibodies, derived from hybridomas constructed by fusion between mouse myeloma and spleen cells from A.TH alloimmune mice (I S anti-I k ), have been used to estimate the allotypic polyporphism of the Ik-gene products. Cross-blocking studies using 17 mAb specific for the I-A molecule indicated that six determinants, which were associated with the conventional specificities Ia.2 and Ia.19, were organized in at least three distinct polymorphic areas of the I-Ak molecules. Similarly, another group of six determinants, which did not correspond to previously described conventional Ia specificities, were found to be topologically heterogeneous. By contrast, the five epitopes associated with the Ia. 1 specificity were clustered into a single region of this molecule. In addition the potentiation of binding observed between mAb specific for topologically distinct epitope regions of the I-Ak molecule, suggested that the latter may undergo conformational changes after binding of a given mAb. A similar analysis of 17 mAb specific for the I-Ek molecule indicated that specificity Ia. 7 of the Eα chain (as defined in this series by eight mAb) was composed of three topologically distinct polymorphic areas, one of which is also spatially related to a complex cluster of eight new determinants of the I-Ek molecule. Finally, one mAb identified a so far undescribed shared determinant of the I-Ak and I-Ek molecules. The present results, which provide a new estimate of the allotypic polymorphism of the Iak antigens, are discussed with regard to their functional, biochemical, and evolutionary implications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00350120
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  • 7
    Electronic Resource
    Electronic Resource
    Murine H-2Dd-reactive monoclonal antibodies recognize shared antigenic determinant(s) on human HLA-B7 or HLA-B27 molecules or both (1983)
    Springer
    Immunogenetics 17 (1983), S. 357-370 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have evaluated the serological relationships between the murine H-2Dd and human HLA molecules using four H-2Dd-reactive monoclonal antibodies (mAbs) produced in the A.BY (KbIbDb) anti-A.TL (KsIkDd) combination. In the mouse, these reagents exhibited three distinct reactivity patterns: Dd, Ks, and H-2u (mAb 81.L); Dd, H-2p, and H-2u (mAb 81.R); and Dd, Kd, H-2p, H-2u, and H-2v (mAbs 97.G and 97.H). Sequential immunoprecipitation and cross-competitive mAb binding experiments revealed that these mAbs recognized determinants in two spatially distinct polymorphic domains on the H-2Dd molecule of B10.A(5R) cells (defined by mAbs 81.L and 81.R, 97.H, and 97.G, respectively). MAbs 81.R, 97.G, and 97.H, but not 81.L, also defined an HLA-linked polymorphism in the human, the main characteristics of which can be summarized as follows: (i) on B lymphoblastoid cell lines, mAbs 81.R and 97.H bound to cells expressing the HLA-B7, HL-B27 or -Bw40 cross-reacting specificities, (ii) on peripheral blood lymphocyte (PBL) panel mAb 81.R exerted C dependent cytotoxicity to 118 of 400 cells tested, including almost all HLA-B7 or HLA-B27 cells or both (r: 0.952), (iii) the expression of the 81.R. cross-reacting determinant segregated in an informative family with the parental haplotype carrying the HLA-B7 allele, and (iv) mAbs 81.R, 97.G, and 97.H recognized topologically related determinants on the same class I molecule(s) of the human B lymphoblastoid cells JY (HLA-A2,2, -B7,7). These data support the view that some, but not all H-2Dd allotopes have been conserved throughout evolution and are associated in the human with the HLA-B7, -B27 cross-reacting specificities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00372455
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of monoclonal antibodies identifying type and strain-specific epitopes of human immunodeficiency virus type 1 (1991)
    Springer
    Molecular and cellular biochemistry 102 (1991), S. 115-123 
    Details
    ISSN: 1573-4919
    Keywords: human immunodeficiency virus ; monoclonal antibodies ; epitope ; viruses subtyping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Several hybridoma cell lines were raised against the highly cytopathic Zairian isolate of Human Immunodeficiency Virus (HIV), HIV1-NDK. The specificity of the secreted monoclonal antibodies (mAb) was demonstrated by immunoblotting, radioimmunoprecipitation and immunofluorescence. Two hybridoma cell lines secreted mAb reacting with independent epitopes of the NDK p17 capsid protein and its precursors. One, RL16.24.5, is specific for the NDK isolate whereas the other, RL16.45.1, along with anti-p25 RL16.30.1 mAb, bind all HIV1 isolates but not HIV2. Together with the previously described mAb RL4.72.1 those reagents define lentivirus subfamily (HIV1, HIV2, SIV) type/subtype (HIV1) and strain (HIVI-NDK) specific epitopes expressed on HIVl-NDK core proteins. The last mAb RL16.76.1 binds the env gene products gp160 and gp120.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00234569
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  • 9
    Electronic Resource
    Electronic Resource
    Genetic control of immune response to staphylococcal nuclease. XII: Analysis of nuclease antigenic determinants using anti-nuclease monoclonal antibodies (1985)
    Springer
    Molecular and cellular biochemistry 68 (1985), S. 31-40 
    Details
    ISSN: 1573-4919
    Keywords: antigenic determinants ; monoclonal antibodies ; staphylococcal nuclease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary SJL mice, which are high responders to Staphylococcal nuclease (nuclease), were immunized and used to produce hybridoma cell lines secreting anti-nuclease monoclonal antibodies (mAb). Ten stable clones were derived from a single fusion. Seven of these produced antibodies of the IgG1,κ isotype and were more precisely characterized for antigenic specificity. Only one hybridoma cell line (54-10-4) produced anti-nuclease antibodies capable of inhibiting enzymatic activity of nuclease. Binding inhibition analyses strongly suggest that the other monoclonal antibodies, which failed to inhibit nuclease activity detect two different antigenic regions, or epitopes, of the molecule: epitope cluster 1 domain is defined by hybridomas 54-2-7, 54-5-2, 54-9-8, and 54-10-8; epitope cluster 2 by 54-5-1 and 54-1-9. Because of its capacity to inhibit nuclease enzymatic activity mAb 54-10-4 was considered specific for a third epitope of the nuclease molecule called epitope 3. Binding studies of these monoclonal antibodies were extended to peptide fragments of the nuclease molecule in order to examine possible cross-reactions with such fragments, as has previously been reported for antibodies purified from polyclonal antisera. Monoclonal antibodies specific for epitope cluster 1 on the native molecule also bound to the fragments 1–126 and 49–149 but failed to bind to fragment 99–149, suggesting that the corresponding epitope(s) is determined by amino acids localized between residues 49 and 99. The epitope clusters 2 and 3 appeared to be expressed only on the native molecule. Monoclonal antibodies of different clusters exhibited very different migration patterns on isoelectric focusing while monoclonal antibodies of the same cluster were indistinguishable, which suggests that they may have originated from the same B cell precursor. Taken together these data suggest that this panel of monoclonal antibodies detects at least three distinct epitopes of the nuclease molecule, one of which could be involved in the determination of the enzymatic site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219386
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  • 10
    Electronic Resource
    Electronic Resource
    Inhibition of the catalytic properties of Staphylococcus aureus nuclease by monoclonal antibodies (1987)
    Springer
    Molecular and cellular biochemistry 74 (1987), S. 117-128 
    Details
    ISSN: 1573-4919
    Keywords: monoclonal antibodies ; hybridoma cell lines ; mice ; antibody repertoire ; Staphylococcus aureus nuclease ; enzyme inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Monoclonal antibodies (Mab) specific for Staphylococcus aureus nuclease (nuclease) were examined for their capacity to inhibit the enzyme-mediated cleavage of DNA. Within a panel of 22 anti-nuclease Mab produced by hybridoma cell lines derived from SJL/J, A/J or BALB/c mice, only five were capable of modifying nuclease activity. Of the five, only one protected DNA from enzymatic degradation whereas the others reduced the rate of the enzymatic reaction. When mixed together, partially inactivating Mabs were frequently more efficient inhibitors than when used individually. It was shown by competitive binding assay that nuclease could be bound simultaneously to more than one Mab. Mixtures of five inactivating Mabs were able to completely block the nuclease activity. Although the actual mechanism for Mab nuclease inactivation is not known, the present data are consistent with simple steric hindrance for the formation of the DNA-nuclease complex by bulky Mab molecules bound to epitopes close to, but distinct from, nuclease catalytic sites. A mathematical model for Mab binding and inactivation of nuclease, taking into account multiple binding events for one or two Mabs interacting with nuclease, was used to derive affinities and maximum reductions of the enzymatic rate (details on the derivation of the equations and on the hypotheses of the model are given in an appendix). This analysis showed that the observed cooperative effects were dependent on the formation of multi-molecular complexes in which nuclease is bound simultaneously to two (or more) different Mabs. It also shows that the formation of cyclic complexes, if allowed, might result in very high apparent affinities. Since in screening of hybridoma fusions, the probability of finding such pairs of monoclonal antibodies would be low, this phenomenon may explain the fact that no Mab, or mixture of Mabs, matched the polyclonal antisera in capacity to block nuclease enzymatic activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00224949
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