A review, with 77 referencesT-cell activation and response to antigen follows presentation by major histocompatibility complex (MHC)-compatible antigen-presenting cells (APC).Activation requires a number of sep. but interrelated receptor-ligand interactions between the T cell and APC.Some of these interactions can be mimicked by other mols., such as lectins, antibodies, or synthetic peptides.We discuss the potential use of conjugates to activate T cells, and describe a new class of heteroconjugates for stimulation or modulation of antigen-specific T-cell activity.These heteroconjugates contain an antigen-specific epitope coupled to a T-cell ligand, which replaces some functions of the APC.Such heteroconjugates would bind and supply two signals to T cells, one through the antigen-recognition site of the T-cell receptor and the other through receptors required for activation.Natural heteroconjugates of this type have been identified, for example in a small peptide derived from a Mycobacterium leprae protein.One coupling of these two signaling moieties into a single soluble mol. may allow antigen-specific T-cell activation without the need for processing and presentation by antigen-presenting cells and without MHC restriction.Conjugates of this type may be useful for the study of T-cell activation, the development of new antigen-specific diagnostic materials and immunomodulators, and possibly a new class of vaccines.

Vaccine Research

Immunization with peptide heteroconjugates primes a T helper cell type 1-associated antibody (IgG2a) response that recognizes the native epitope on the 38-kDa protein of Mycobacterium tuberculosis

Author: Worthington, Kirby F. W. ; Elliott, Donald A. ; Rouse, David ; Morris, Sheldon ; Zimmerman, Daniel H. ; Rosenthal, Kenneth S.

Heteroconjugates were prepared by covalently linking a peptide (M) bearing the 38.G epitope from the 38-kDa protein (residues 350-369) of Mycobacterium tuberculosis, to peptides containing T-cell binding ligands (TCBL) or keyhole limpet hemocyanin (KLH).BALB/c mice were immunized with the heteroconjugates using incomplete Freund's adjuvant (ICFA) supplemented with muramyl dipeptide.The resultant antisera were analyzed by ELISA (ELISA) procedures.Antibody titers and serotype were used as indicators of involvement and modulation of T-helper (Th) activity.Initial immunization and challenge with the TCBL-containing heteroconjugates did not elicit specific antibody to the M peptide (38.G epitope); however, a heteroclitic response was generated.The peptide conjugated to KLH (M-KLH) elicited specific anti-M antibody.Specific antibody was elicited following challenge of animals primed with the TCBL heteroconjugate and then challenged with M-KLH.The response was unlike unprimed mice, or animals primed with peptide M or control heteroconjugates.The antibody subtypes produced against peptide M were consistent with a Th1 response (IgG2a) for the heteroconjugates containing major histocompatibility complex (MHC) class I TCBL and Th2 responses (IgG1) for those containing MHC class II T-cell binding ligands or KLH.Immunoblot anal. indicated that these TCBL heteroconjugate-associated antibodies recognized the 38.G epitope in the 38-kDa protein of M. tuberculosis (reduced-SDS-denatured protein).However, unlike the TCBL-heteroconjugate-induced antibodies, the anti-peptide 38.G antibodies elicited from M-KLH-primed animals were unable to recognize the epitope in extracts containing the native protein from sonicated bacteria.ELISA studies indicated that the heteroconjugate-induced IgG2a antibodies recognized the 38.G epitope on the native protein in sonicates of various Mycobacterium sps.The results for M-peptide-TCBL heteroconjugates mimic a natural rechallenge and suggest that memory cells were elicited by the initial priming immunization.The implications of preferential stimulation of specific Th cell subsets, selective production of defined IgG subclass antibodies, and antibodies reactive against a native tuberculosis disease-related protein from different strains are discussed.

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