PMID- 10430630
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20191023
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 190
IP  - 3
DP  - 1999 Aug 2
TI  - The majority of H2-M3 is retained intracellularly in a peptide-receptive state
      and traffics to the cell surface in the presence of N-formylated peptides.
PG  - 423-34
AB  - We used a new monoclonal antibody (mAb 130) to analyze the intracellular
      trafficking and surface expression of H2-M3, the major histocompatibility complex
      class Ib molecule that presents N-formylated peptides to cytotoxic T cells. M3
      surface expression is undetectable in most cell types due to the paucity of
      endogenous antigen. M3 is induced on the cell surface by addition of
      high-affinity N-formylated peptides from mitochondria and listeria.
      Peptide-induced M3 expression is most efficient on antigen presenting cells.
      Basal and inducible expression of M3 is transporter associated with antigen
      processing (TAP)-dependent, distinguishing M3 from the class Ib molecules TL and 
      CD1. Unlike the expression of class Ia molecules and a previously described
      M3/L(d) chimera, surface expression of M3 cannot be rescued by lowered
      temperature, suggesting that the alpha3 domain and transmembrane region of M3 may
      control trafficking. Pulse-chase analysis and use of trafficking inhibitors
      revealed a pool of empty M3 in the endoplasmic reticulum or early Golgi
      apparatus. Addition of exogenous peptide allows maturation with kinetics matching
      those of D(d). The lack of endogenous N-formylated peptide allows discovery of
      novel pathogen-derived peptides in normal antigen presenting cells. The
      nonpolymorphic nature of M3 and its ability to present bacterial antigens rapidly
      and dominantly make it an attractive target for peptide vaccination strategies.
FAU - Chiu, N M
AU  - Chiu NM
AD  - Gwen Knapp Center for Lupus and Immunology Research, Committee on Immunology,
      Department of Pathology, University of Chicago, Illinois 60637, USA.
FAU - Chun, T
AU  - Chun T
FAU - Fay, M
AU  - Fay M
FAU - Mandal, M
AU  - Mandal M
FAU - Wang, C R
AU  - Wang CR
LA  - eng
GR  - K08 MH090397/MH/NIMH NIH HHS/United States
GR  - R29 AI040310/AI/NIAID NIH HHS/United States
GR  - R29 AI040310-05/AI/NIAID NIH HHS/United States
GR  - AI40310/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (ATP Binding Cassette Transporter, Subfamily B, Member 2)
RN  - 0 (ATP-Binding Cassette Transporters)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (H2-M3 antigen)
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (Membrane Proteins)
RN  - 0 (Oligopeptides)
RN  - 0 (Protein Synthesis Inhibitors)
RN  - 0 (TAP1 protein, human)
RN  - 0 (Tap1 protein, mouse)
RN  - 4289-98-9 (N-Formylmethionine)
SB  - IM
MH  - ATP Binding Cassette Transporter, Subfamily B, Member 2
MH  - ATP-Binding Cassette Transporters/pharmacology
MH  - Animals
MH  - Antibodies, Monoclonal/biosynthesis/pharmacology
MH  - Antigen Presentation/drug effects
MH  - Biological Transport/immunology
MH  - Cell Line
MH  - Cell Membrane/immunology/metabolism
MH  - Cricetinae
MH  - Histocompatibility Antigens Class I/biosynthesis/immunology/*metabolism
MH  - Intracellular Fluid/immunology/*metabolism
MH  - Kinetics
MH  - Lymphoid Tissue/cytology/immunology/metabolism
MH  - Membrane Proteins/biosynthesis/immunology/*metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - N-Formylmethionine/*metabolism
MH  - Oligopeptides/immunology/*metabolism/physiology
MH  - Protein Synthesis Inhibitors/pharmacology
PMC - PMC2195588
EDAT- 1999/08/03 00:00
MHDA- 1999/08/03 00:01
CRDT- 1999/08/03 00:00
PHST- 1999/08/03 00:00 [pubmed]
PHST- 1999/08/03 00:01 [medline]
PHST- 1999/08/03 00:00 [entrez]
AID - 10.1084/jem.190.3.423 [doi]
PST - ppublish
SO  - J Exp Med. 1999 Aug 2;190(3):423-34. doi: 10.1084/jem.190.3.423.