T cell recognition of antigen in vivo: Role of the H-2 complex

1980 ◽  
Vol 3 (2) ◽  
pp. 213-245 ◽  
Author(s):  
J. Sprent ◽  
R. Korngold ◽  
K. Molnar-Kimber
2008 ◽  
Vol 181 (11) ◽  
pp. 7721-7727 ◽  
Author(s):  
Amy K. Wesa ◽  
Christopher J. Herrem ◽  
Maja Mandic ◽  
Jennifer L. Taylor ◽  
Cecilia Vasquez ◽  
...  

1987 ◽  
Vol 43 (1) ◽  
pp. 228-240 ◽  
Author(s):  
Michael J Owen ◽  
Michael J Crumpton

1996 ◽  
Vol 26 (4) ◽  
pp. 768-772 ◽  
Author(s):  
Kim I. Dawe ◽  
Patricia R. Hutchings ◽  
Mario Geysen ◽  
Brian R. Champion ◽  
Anne Cooke ◽  
...  

Nature ◽  
1985 ◽  
Vol 317 (6036) ◽  
pp. 425-427 ◽  
Author(s):  
Hana Golding ◽  
James McCluskey ◽  
Terry I. Munitz ◽  
Ronald N. Germain ◽  
David H. Margulies ◽  
...  

1979 ◽  
Vol 149 (5) ◽  
pp. 1208-1226 ◽  
Author(s):  
A Singer ◽  
K S Hathcock ◽  
R J Hodes

Requirements for helper T-cell recognition of H-2 determinants expressed on adherent accessory cells and on B cells was individually assessed in the anti-hapten PFC responses to TNP-KLH. Complicating allogeneic effects were minimized or avoided by the use of helper T cells from normal F1 hybrids, parent leads to F1 chimeras, and F1 leads to parent chimeras. The results of both in vitro and in vivo experiments demonstrated that: (a) helper T cells are not required to recognize the identical H-2 determinants on both accessory cells and B cells; (b) helper T cells are required to recognize K or I-A region-encoded determinants expressed on accessory cells; (c) no requirement was observed in vitro or in vivo for helper T-cell recognition of B-cell-expressed H-2 determinants; and (d) no requirement was observed for H-2 homology between accessory cells and B cells. The absence of required helper T-cell recognition of the identical H-2 determinants on both accessory cells and B cells was demonstrated in two ways: (a) naive of KLH-primed (A x B)F1 hybrid helper T cells collaborated equally well with B cells from either parentA or parentB in the presence of accessory cells from either parent; (b) A leads to (A x B)F1 chimeric spleen cells depleted of accessory cells collaborated equally well with accessory cells from either parentA or parentB, even though the B cells only expressed the H-2 determinants of parentA. A requirement for helper T-cell recognition of K or I-A region-encoded H-2 determinants on accessory cells was also demonstrated in two ways: (a) (A x B)F1 leads to parentA chimeric spleen cells depleted of accessory cells collaborated with accessory cells from parentA but not parentB; and (b) (A x B)F1 leads to parentA chimeric helper T cells collaborated with normal F1 B cells only in the presence of parental or recombinant accessory cells that expressed the K or I-A region-encoded determinants of parentA. Although restricted in their ability to recognize H-2 determinants on accessory cells, it was demonstrated both in vitro and in vivo that (A x B)F1 leads to parentA chimeric helper T cells were able to collaborate with B cells from either parentA or parentB. In vitro in the presence of accessory cells from parentA, (A x B)F1 leads to parentA chimeric helper T cells collaborated equally well with B cells from either parent. In addition, the inability of (A x B)F1 leads to parentA chimeric helper T cells to collaborate with (B + accessory) cells from parentB was successfully reversed by the addition of parentA SAC as added accessory cells. In vivo, upon the addition of parentA accessory cells, (A x B)F1 leads to parentA chimeric helper T cells collaborated with parentB B cells in short-term adoptive transfer experiments.


1987 ◽  
Vol 25 (3) ◽  
Author(s):  
CarinaM. Henningsson ◽  
Subnaicker Selvaraj ◽  
GrantD. MacLean ◽  
MavanurR. Suresh ◽  
AntoineA. Noujaim ◽  
...  

2007 ◽  
Vol 75 (6) ◽  
pp. 2914-2921 ◽  
Author(s):  
Annemieke Geluk ◽  
May Young Lin ◽  
Krista E. van Meijgaarden ◽  
Eliane M. S. Leyten ◽  
Kees L. M. C. Franken ◽  
...  

ABSTRACT During stationary growth or in vitro conditions mimicking relevant aspects of latency, the HspX protein (Rv2031c) is specifically upregulated by Mycobacterium tuberculosis. In this study we compared T-cell responses against HspX and the secreted M. tuberculosis protein Ag85B (Rv1886c) in tuberculosis (TB) patients, tuberculin skin test-positive individuals, M. bovis BCG-vaccinated individuals, and healthy negative controls. Gamma interferon responses to HspX were significantly higher in M. tuberculosis-exposed individuals than in M. tuberculosis-unexposed BCG vaccinees. In contrast, no such differences were found with respect to T-cell responses against Ag85B. Therefore, BCG-based vaccines containing relevant fragments of HspX may induce improved responses against this TB latency antigen. To identify relevant major histocompatibility complex class I- and class II-restricted HspX-specific T-cell epitopes, we immunized HLA-A2/Kb and HLA-DR3.Ab0 transgenic (tg) mice with HspX. Two new T-cell epitopes were identified, p91-105 and p31-50, restricted via HLA-A*0201 and HLA-DRB1*0301, respectively. These epitopes were recognized by human T cells as well, underlining the relevance of HspX T-cell recognition both in vivo and in vitro. In line with the data in humans, BCG immunization of both tg strains did not lead to T-cell responses against HspX-derived epitopes, whereas nonlatency antigens were efficiently recognized. These data support the notion that BCG vaccination per se does not induce T-cell responses against the latency antigen, HspX. Thus, we suggest that subunit vaccines incorporating HspX and/or other latency antigens, as well as recombinant BCG strains expressing latency antigens need to be considered as new vaccines against TB.


2000 ◽  
Vol 192 (7) ◽  
pp. 965-976 ◽  
Author(s):  
D. Branch Moody ◽  
Mark R. Guy ◽  
Ethan Grant ◽  
Tan-Yun Cheng ◽  
Michael B. Brenner ◽  
...  

T cells recognize microbial glycolipids presented by CD1 proteins, but there is no information regarding the generation of natural glycolipid antigens within infected tissues. Therefore, we determined the molecular basis of CD1b-restricted T cell recognition of mycobacterial glycosylated mycolates, including those produced during tissue infection in vivo. Transfection of the T cell receptor (TCR) α and β chains from a glucose monomycolate (GMM)-specific T cell line reconstituted GMM recognition in TCR-deficient T lymphoblastoma cells. This TCR-mediated response was highly specific for natural mycobacterial glucose-6-O-(2R, 3R) monomycolate, including the precise structure of the glucose moiety, the stereochemistry of the mycolate lipid, and the linkage between the carbohydrate and the lipid. Mycobacterial production of antigenic GMM absolutely required a nonmycobacterial source of glucose that could be supplied by adding glucose to media at concentrations found in mammalian tissues or by infecting tissue in vivo. These results indicate that mycobacteria synthesized antigenic GMM by coupling mycobacterial mycolates to host-derived glucose. Specific T cell recognition of an epitope formed by interaction of host and pathogen biosynthetic pathways provides a mechanism for immune response to those pathogenic mycobacteria that have productively infected tissues, as distinguished from ubiquitous, but innocuous, environmental mycobacteria.


1990 ◽  
Vol 87 (7) ◽  
pp. 2603-2607 ◽  
Author(s):  
S. Koyasu ◽  
T. Lawton ◽  
D. Novick ◽  
M. A. Recny ◽  
R. F. Siliciano ◽  
...  

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