PMID- 8641784
OWN - NLM
STAT- MEDLINE
DCOM- 19960716
LR  - 20231213
IS  - 0019-9567 (Print)
IS  - 1098-5522 (Electronic)
IS  - 0019-9567 (Linking)
VI  - 64
IP  - 3
DP  - 1996 Mar
TI  - Differential interaction with endocytic and exocytic pathways distinguish 
      parasitophorous vacuoles of Coxiella burnetii and Chlamydia trachomatis.
PG  - 796-809
AB  - Coxiella burnetii and Chlamydia trachomatis are bacterial obligate intracellular 
      parasites that occupy distinct vacuolar niches within eucaryotic host cells. We 
      have employed immunofluorescence, cytochemistry, fluorescent vital stains, and 
      fluid-phase markers in conjunction with electron, confocal, and conventional 
      microscopy to characterize the vacuolar environments of these pathogens. The 
      acidic nature of the C. burnetii-containing vacuole was confirmed by its 
      acquisition of the acidotropic base acridine orange (AO). The presence of the 
      vacuolar-type (H+) ATPase (V-ATPase) within the Coxiella vacuolar membrane was 
      demonstrated by indirect immunofluorescence, and growth of C. burnetii was 
      inhibited by bafilomycin A1 (Baf A), a specific inhibitor of the V-ATPase. In 
      contrast, AO did not accumulate in C. trachomatis inclusions nor was the V-ATPase 
      found in the inclusion membrane. Moreover, chlamydial growth was not inhibited by 
      Baf A or the lysosomotropic amines methylamine, ammonium chloride, and 
      chloroquine. Vacuoles harboring C. burnetii incorporated the fluorescent fluid- 
      phase markers, fluorescein isothiocyanate-dextran (FITC-dex) and Lucifer yellow 
      (LY), indicating trafficking between that vacuole and the endocytic pathway. 
      Neither FITC-dex nor LY was sequestered by chlamydial inclusions. The late 
      endosomal-prelysosomal marker cation-independent mannose 6-phosphate receptor was 
      not detectable in the vacuolar membranes encompassing either parasite. However, 
      the lysosomal enzymes acid phosphatase and cathepsin D and the lysosomal 
      glycoproteins LAMP-1 and LAMP-2 localized to the C. burnetii vacuole but not the 
      chlamydial vacuole. Interaction of C. trachomatis inclusions with the 
      Golgi-derived vesicles was demonstrated by the transport of sphingomyelin, 
      endogenously synthesized from C6-NBD-ceramide, to the chlamydial inclusion and 
      incorporation into the bacterial cell wall. Similar trafficking of C-NBD-ceramide 
      was not evident in C. burnetii-infected cells. Collectively, the data indicate 
      that C. trachomatis replicates within a nonacidified vacuole that is disconnected 
      from endosome-lysosome trafficking but may receive lipid from exocytic vesicles 
      derived from the trans-Golgi network. These observations are in sharp contrast to 
      those for C. burnetii, which by all criteria resides in a typical phagolysosome.
FAU - Heinzen, R A
AU  - Heinzen RA
AD  - Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National 
      Institute of Allergy and Infectious Diseases, Hamilton, Montana 59840-2999,USA.
FAU - Scidmore, M A
AU  - Scidmore MA
FAU - Rockey, D D
AU  - Rockey DD
FAU - Hackstadt, T
AU  - Hackstadt T
LA  - eng
GR  - N01-HD-2-3144/HD/NICHD 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  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Antigens, CD)
RN  - 0 (Lysosomal Membrane Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Sphingolipids)
SB  - IM
MH  - Animals
MH  - Antigens, CD/metabolism
MH  - Chlamydia trachomatis/metabolism/*ultrastructure
MH  - Chlorocebus aethiops
MH  - Coxiella burnetii/metabolism/*ultrastructure
MH  - *Endocytosis
MH  - *Exocytosis
MH  - Humans
MH  - Lysosomal Membrane Proteins
MH  - Lysosomes/enzymology
MH  - Membrane Glycoproteins/metabolism
MH  - Mice
MH  - Rabbits
MH  - Sphingolipids/metabolism
MH  - Vacuoles/*metabolism
MH  - Vero Cells
PMC - PMC173840
EDAT- 1996/03/01 00:00
MHDA- 1996/03/01 00:01
PMCR- 1996/03/01
CRDT- 1996/03/01 00:00
PHST- 1996/03/01 00:00 [pubmed]
PHST- 1996/03/01 00:01 [medline]
PHST- 1996/03/01 00:00 [entrez]
PHST- 1996/03/01 00:00 [pmc-release]
AID - 10.1128/iai.64.3.796-809.1996 [doi]
PST - ppublish
SO  - Infect Immun. 1996 Mar;64(3):796-809. doi: 10.1128/iai.64.3.796-809.1996.