PMID- 7533085
OWN - NLM
STAT- MEDLINE
DCOM- 19950406
LR  - 20131121
IS  - 0014-2980 (Print)
IS  - 0014-2980 (Linking)
VI  - 25
IP  - 2
DP  - 1995 Feb
TI  - Intracellular processing and presentation of T cell epitopes, expressed by 
      recombinant Escherichia coli and Salmonella typhimurium, to human T cells.
PG  - 405-10
AB  - Vaccines based on recombinant attenuated bacteria represent a potentially safe 
      and effective immunization strategy. A carrier system was developed to analyze in 
      vitro whether foreign T cell epitopes, inserted in the outer membrane protein 
      PhoE of Escherichia coli and expressed by recombinant bacteria, are efficiently 
      processed and presented via human leukocyte antigen (HLA) class I and II 
      molecules by bacterial infected human macrophages. A well-defined 
      HLA-B27-restricted cytotoxic T cell (CTL) epitope and an HLA-DR53 restricted T 
      helper (Th) epitope of the fusion protein of measles virus were genetically 
      inserted in a surface-exposed region of PhoE, and the chimeric proteins were 
      expressed in E. coli and Salmonella typhimurium. Macrophages infected with both 
      recombinant bacteria presented the Th epitope to the specific CD4+ T cell clone, 
      but failed to present the CTL epitope to the specific CD8+ T cell clone. 
      Presentation of the Th epitope by the infected macrophages was inhibited by 
      cytochalasin D, indicating that phagocytic processing of intact bacteria within 
      infected macrophages was essential for antigen presentation via HLA class II. 
      Presentation of the Th epitope to the CD4+ T cell clone by infected macrophages 
      was blocked by brefeldin A and cycloheximide, indicating the requirement of 
      nascent HLA class II molecules for presentation. The efficiency of macrophages to 
      process and present the inserted Th epitope was similar for both the recombinant 
      E. coli and S. typhimurium strains.
FAU - Verjans, G M
AU  - Verjans GM
AD  - Department of Ophthalmo-Immunology, Netherlands Ophthalmic Research Institute, 
      Amsterdam.
FAU - Janssen, R
AU  - Janssen R
FAU - UytdeHaag, F G
AU  - UytdeHaag FG
FAU - van Doornik, C E
AU  - van Doornik CE
FAU - Tommassen, J
AU  - Tommassen J
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Eur J Immunol
JT  - European journal of immunology
JID - 1273201
RN  - 0 (Cyclopentanes)
RN  - 0 (Epitopes)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Porins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Viral Proteins)
RN  - 20350-15-6 (Brefeldin A)
RN  - 22144-77-0 (Cytochalasin D)
RN  - 85130-31-0 (PhoE protein, E coli)
RN  - 98600C0908 (Cycloheximide)
SB  - IM
MH  - Amino Acid Sequence
MH  - *Antigen Presentation
MH  - Base Sequence
MH  - Brefeldin A
MH  - Cycloheximide/pharmacology
MH  - Cyclopentanes/pharmacology
MH  - Cytochalasin D/pharmacology
MH  - *Epitopes
MH  - Escherichia coli/genetics
MH  - Escherichia coli Proteins
MH  - Humans
MH  - Macrophages/*metabolism
MH  - Molecular Sequence Data
MH  - Porins/metabolism
MH  - Recombinant Fusion Proteins/*metabolism
MH  - Salmonella typhimurium/genetics
MH  - T-Lymphocytes/*immunology
MH  - Viral Proteins/immunology
EDAT- 1995/02/01 00:00
MHDA- 1995/02/01 00:01
CRDT- 1995/02/01 00:00
PHST- 1995/02/01 00:00 [pubmed]
PHST- 1995/02/01 00:01 [medline]
PHST- 1995/02/01 00:00 [entrez]
AID - 10.1002/eji.1830250215 [doi]
PST - ppublish
SO  - Eur J Immunol. 1995 Feb;25(2):405-10. doi: 10.1002/eji.1830250215.