Cited by 356Cellular transport and secretionTuberculosis Research and EpidemiologyMycobacterium research and diagnosis

Mycobacterium‐containing phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis.

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Sturgill‐Koszycki, S., Schaible, U. E., Russell, D. G.·1996·The EMBO Journal

Abstract

The success of Mycobacterium as a pathogen hinges on its ability to modulate its intracellular environment. Mycobacterium avium reside in vacuoles with limited proteolytic activity, maintain cathepsin D in an immature form and remain accessible to internalized transferrin. Artificial acidification of isolated phagosomes facilitated processing of cathepsin D, demonstrating that pH alone limits proteolysis in these vacuoles. Moreover, analysis of IgG-bead phagosomes at early time points during their formation indicates that these phagosomes also acquire LAMP 1 and cathepsin D prior to the accumulation of proton-ATPases, and are transiently accessible to sorting endosomes. This suggests that the anomolous distribution of endosomal proteins in M. avium-containing vacuoles results from their arrested differentiation in an early transitional stage through which all phagosomes pass.

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Crossref · 10.1002/j.1460-2075.1996.tb01088.x

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  • Some hydrolases such as cathepsin D depend on further processing by other proteases and/or autocatalysis to generate the enzymatically active forms.

    “Some of those such as cathepsin D depend on further processing by other proteases and/or autocatalysis to generate the enzymatically active forms (40).”

    From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [40]

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References 51 · Cited by 356

Authors
Sturgill‐Koszycki, S., Schaible, U. E., & Russell, D. G.
Affiliations
Washington University in St. Louis (US)
Venue
The EMBO Journal
Published
1996-12-01
Volume
15
Issue
24
Pages
6960-6968
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
OpenAlex
W2296824252
Cited by
356
References
51
Citations by year
2026: 2 · 2025: 1 · 2024: 3 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 8 · 2018: 5 · 2017: 7 · 2016: 6 · 2015: 6 · 2014: 12 · 2013: 11 · 2012: 12
FWCI
7.35
Type
journal article
Language
en
Open access
Locations
  • The EMBO Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Public Health Service
  • National Heart, Lung, and Blood Institute (R01HL055936, HL-55936)
  • National Institute of Allergy and Infectious Diseases (AI-33348, P01AI033348)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
  • Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
Keywords
Mycobacterium avium, phagosome biogenesis, early endosomes, cathepsin D, LAMP1, phagosome acidification, proteolysis, transferrin, H+-ATPase
MeSH terms
Animals, Cathepsin D, Proton-Translocating ATPases, Hydrogen-Ion Concentration, Immunoglobulin G, Mice, Inbred BALB C, Mycobacterium avium, Phagosomes, Protein Processing, Post-Translational, Endosomes, Vacuoles, Microscopy, Immunoelectron, Mice

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