PMID- 10092778
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20111117
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 162
IP  - 6
DP  - 1999 Mar 15
TI  - Phagosomes are fully competent antigen-processing organelles that mediate the
      formation of peptide:class II MHC complexes.
PG  - 3263-72
AB  - During the processing of particulate Ags, it is unclear whether peptide:class II 
      MHC (MHC-II) complexes are formed within phagosomes or within endocytic
      compartments that receive Ag fragments from phagosomes. Murine macrophages were
      pulsed with latex beads conjugated with OVA. Flow or Western blot analysis of
      isolated phagosomes showed extensive acquisition of MHC-II, H-2M, and invariant
      chain within 30 min, with concurrent degradation of OVA. T hybridoma responses to
      isolated subcellular fractions demonstrated OVA (323-339):I-Ad complexes in
      phagosomes and plasma membrane but not within dense late endocytic compartments. 
      Furthermore, when two physically separable sets of phagosomes were present within
      the same cells, OVA(323-339):I-Ad complexes were demonstrated in latex-OVA
      phagosomes but not in phagosomes containing latex beads conjugated with another
      protein. This implies that these complexes were formed specifically within
      phagosomes and were not formed elsewhere and subsequently transported to
      phagosomes. In addition, peptide:MHC-II complexes were shown to traffic from
      phagosomes to the cell surface. In conclusion, phagosomes are fully competent to 
      process Ags and generate peptide:MHC-II complexes that are transported to the
      cell surface and presented to T cells.
FAU - Ramachandra, L
AU  - Ramachandra L
AD  - Institute of Pathology, Case Western Reserve University, Cleveland, OH 44106,
      USA.
FAU - Song, R
AU  - Song R
FAU - Harding, C V
AU  - Harding CV
LA  - eng
GR  - AI34343/AI/NIAID NIH HHS/United States
GR  - AI35726/AI/NIAID NIH HHS/United States
GR  - CA70149/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (H2-M antigens)
RN  - 0 (HLA-D Antigens)
RN  - 0 (HLA-DM antigens)
RN  - 0 (Histocompatibility Antigens Class II)
RN  - 0 (Lysosome-Associated Membrane Glycoproteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (OVA 323-339)
RN  - 0 (Peptide Fragments)
RN  - 0 (Peptides)
RN  - 0 (invariant chain)
RN  - 9006-59-1 (Ovalbumin)
RN  - EC 3.2.1.17 (Muramidase)
SB  - AIM
SB  - IM
MH  - Animals
MH  - *Antigen Presentation
MH  - Antigens, CD/biosynthesis
MH  - Antigens, Differentiation, B-Lymphocyte/analysis
MH  - Biological Transport/immunology
MH  - Blotting, Western
MH  - Cell Fractionation
MH  - Cell Membrane/immunology/metabolism
MH  - Centrifugation, Density Gradient
MH  - Flow Cytometry
MH  - HLA-D Antigens/analysis
MH  - Histocompatibility Antigens Class II/analysis/biosynthesis/*metabolism
MH  - Lysosome-Associated Membrane Glycoproteins
MH  - Macromolecular Substances
MH  - Macrophages, Peritoneal/immunology/metabolism
MH  - Membrane Glycoproteins/biosynthesis
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Inbred DBA
MH  - Mice, Knockout
MH  - Mice, Transgenic
MH  - Microspheres
MH  - Muramidase/analysis
MH  - Ovalbumin/immunology/metabolism
MH  - Peptide Fragments/immunology/metabolism
MH  - Peptides/immunology/*metabolism
MH  - Phagosomes/enzymology/*immunology/*metabolism
MH  - Subcellular Fractions/chemistry
MH  - T-Lymphocytes/chemistry
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1999 Mar 15;162(6):3263-72.