Lymphoid Cell Surface Interaction Structures Detected Using Cytolysis‐Inhibiting Monoclonal Antibodies

Abstract

We screened monoclonal antibodies obtained by xenogeneic immunization for their capacity to inhibit T cell-mediated cytolysis. These antibodies fell into two classes according to the cell structures they recognized, of 30-35 K and 94-180 K apparent molecular weight, respectively. The main features of these structures and of their interaction with the corresponding antibodies were reviewed. The inhibition of cytolysis by these antibodies was shown to occur mainly at the effector cell level, at the recognition stage of cytolysis, and to depend on the nature of target cells, effector cells, and link between these cells. T cell functions other than cytolysis were also inhibited by some of these antibodies. We considered various possible mechanisms to account for the inhibition of cytolysis by these mAb. We favor an hypothesis based on inhibition by these mAb of lymphoid cell surface interaction structures. This hypothesis was discussed within the general framework of cell interaction structures in immunological and non-immunological experimental systems.

Expression, Purification, and Functional Analysis of Murine Ectodomain Fragments of CD8αα and CD8αβ Dimers

“…2B, the immunoaffinity purified mCD8␣␤-LZ material is ϳ90% pure. The 2H11 mAb-purified mCD8␣␤-LZ protein expresses the native epitopes recognized by five distinct anti-CD8␣ mAbs (53.6.72, 19/178, H59 -101.7, YTS105, and YTS169) (34,35,39) and four anti-CD8␤ mAbs (53.5.8, H35-17, YTS156.7, and KT112) (34,35,39,40), as measured by BIAcore binding studies (data not shown).…”

Cytotoxic T cell response to Mengo virus in mice: effector cell phenotype and target proteins

“…Effector cells (107 cells/ml) were incubated for 1 h at 4 °C in R2 medium (R5 medium with 2 % FCS) containing 10 gg/ml of rat MAbs GK1.5 (Dialynas et al, 1983) or H35.17.2 (Golstein et al, 1982). They were then washed twice with cold R2 medium, resuspended in cold R0 medium containing 108 sheep anti-rat lgG dynabeads/ml (Dynal) and further incubated for 1 h at 4 °C.…”

The Majority of Infiltrating CD8+T Cells in the Central Nervous System of Susceptible SJL/J Mice Infected with Theiler's Virus Are Virus Specific and Fully Functional

“…2A). The results clearly indicate that the CD8 ϩ T-cell fraction recognizes the VP1 [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30] , VP3 151-170 , and VP3 [171][172][173][174][175][176][177][178][179][180][181][182][183][184][185][186][187][188][189][190] peptides. As expected, the CD4 ϩ T-cell fraction produced IFN-␥ in response to known Th epitope-containing peptides, VP1 231-250 and VP3 [21][22][23][24][25][26][27][28][29][30][31][32][33][34]<...>…”

“…Figure 1 represents a typical profile of the consistent pattern of IFN-␥ production by CNS-IL at an early stage (7 to 10 days) of TMEV infection. Interestingly, the VP3 151-170 , VP3 [171][172][173][174][175][176][177][178][179][180][181][182][183][184][185][186][187][188][189][190] , and VP1 [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30] peptides stimulated noticeably higher numbers of IFN-␥-producing cells than the VP2 71-90 , VP3 [21][22][23][24][25][26][27][28][29][30][31][32]…”

“…Definition of class I-restricted minimal epitopes by using truncated peptides. To determine the minimal epitopes within the 20-mer peptides used above, we generated truncated forms of the 20-mer peptides (VP1 [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30] , VP3 151-170 , and VP3 [171][172][173][174][175][176][177][178][179][180][181][182][183][184][185][186][187][188][189][190] ) and assessed which regions are required for T-cell stimulation. Initially, we used peptides truncated by 2 amino acids each to define the N terminus (Fig.…”