Nature of T lymphocyte recognition of macrophage-associated antigens

Thomas, David W.; Schauster, John L.; Wilner, George D.

doi:10.1016/0008-8749(81)90217-3

Cited by 8 publications

(1 citation statement)

References 8 publications

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“…T cells from insulin B chain-primed guinea pigs recognize an octapeptide from that molecule (18), whereas a nonapeptide of myelin basic protein is seen by T cells from guinea pigs with experimental allergic encephalomyelitis (19). Similarly, murine T cells primed to myoglobin were stimulated in vitro by 13-residue synthetic fragments of the molecule (20).…”

Section: Resultsmentioning

confidence: 99%

Human T-lymphocyte response in vitro to synthetic peptides of herpes simplex virus glycoprotein D.

DeFreitas¹,

Dietzschold²,

Koprowski³

1985

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

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Immunization of mice with a synthetic peptide that corresponds to a murine antibody-defined immunodominant domain of herpes simplex virus (HSV) glycoprotein D (gD) induced neutralizing antibodies against HSV types 1 and 2 and protected animals against a lethal challenge with HSV type 2 (Dietzschold, B., Eisenberg, R., Ponce de Leon, M., Golub, E., Hudecz, F., Varicchio, A. & Cohen, G. (1984) J. Virol. 52,[431][432][433][434][435]. We report here that human peripheral blood T cells from HSV-seropositive and -seronegative adult donors are activated by this synthetic peptide in vitro. Interleukin-2-dependent T-cell lines established from these cultures respond specifically to peptides containing residues 1-23 of HSV gD and to a panel of overlapping peptides within this domain. The T-cell proliferative response was maximal when the majority of interleukin-2-propagated T cells were of the helper phenotype and the peptides were at least 16 amino acids long. Peptides of 8 or 12 amino acids from the carboxyl terminus were nonstimulatory. Peptide-activated T-cell lines from seronegative donors less than 11 years old could be established in vitro, but most cells were of the suppressor/cytotoxic phenotype and demonstrated no antigen-specificity when tested with the panel of synthetic peptides.The immune response to herpes simplex virus (HSV) has been shown to involve a variety of effector mechanisms which include production of virus-neutralizing antibody, cytotoxic T lymphocytes, natural killer (NK) cells, antibodydependent cellular cytotoxicity, and T-cell-derived lymphokines (43). The pivotal role of helper T-cells in the induction of these responses has been well documented (44,45).The nature of the HSV-specified antigens that act as immunostimulants has not been completely identified, but several lines of evidence implicate the major viral glycoproteins (1). One of these, glycoprotein D (gD), has been shown to induce type-common viral-neutralizing antibody (2, 3), and passive administration of monoclonal antibody (mAb) specific for gD protects mice from a lethal challenge with HSV (4). Moreover, gD appears to be recognized on HSV-infected cells by cytolytic effector cells (5).An antibody-defined immunodominant determinant of HSV type 1 (HSV-1) gD was localized and a peptide corresponding to residues 8-23 of the mature glycoprotein was synthesized. This peptide was recognized by an anti-gD mAb known to neutralize HSV-1 and -2 (6). Moreover, immunization of mice with this synthetic molecule induces viral-neutralizing antibodies and confers protection against a lethal challenge with HSV-2 (7). MATERIALS AND METHODSSynthesis of HSV gD Peptides. Peptides were manually synthesized as described (6) by using the Merrifield solidphase method (8). The completed peptides were simultaneously deprotected and cleaved from the resin with anhydrous HF containing thioanisole as an organic cation scavenger. The crude peptides were purified by gel filtration on Bio-Gel P-2 or P-4 (Bio-Rad) columns. Homogeneity of the peptides w...

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Section: Resultsmentioning

confidence: 99%

Human T-lymphocyte response in vitro to synthetic peptides of herpes simplex virus glycoprotein D.

DeFreitas¹,

Dietzschold²,

Koprowski³

1985

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

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Peptide binding and antigen presentation by class II histocompatibility glycoproteins

Jensen

1997

Biopolymers

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The immune system has evolved complex mechanisms for the recognition and elimination of pathogens. CD4+ helper T lymphocytes play a central role in orchestrating immune responses and their activation is carefully regulated. These cells selectively recognize short peptide antigens stably associated with membrane‐bound class II histocompatibility glycoproteins that are selectively expressed in specialized antigen presenting cells. The class II—peptide complexes are generated through a series of events that occur in membrane‐bound compartments within antigen presenting cells that, collectively, have become known as the class II antigen processing pathway. In the present paper, our current understanding of this pathway is reviewed with emphasis on mechanisms that regulate peptide binding by class II histocompatibility molecules. © 1997 John Wiley & Sons, Inc. Biopoly 43: 303–322, 1997

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T Lymphocyte Recognition of Small Peptide Antigens: Formation of Neoantigenic Determinants and Clonal Frequency Resulting in IR Gene Control

Thomas

Hoffman

Hsieh

et al. 1983

Protein Conformation as an Immunological Signal

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Nature of T lymphocyte recognition of macrophage-associated antigens

Cited by 8 publications

References 8 publications

Human T-lymphocyte response in vitro to synthetic peptides of herpes simplex virus glycoprotein D.

Human T-lymphocyte response in vitro to synthetic peptides of herpes simplex virus glycoprotein D.

Peptide binding and antigen presentation by class II histocompatibility glycoproteins

T Lymphocyte Recognition of Small Peptide Antigens: Formation of Neoantigenic Determinants and Clonal Frequency Resulting in IR Gene Control

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