For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
11
views
13
references
 Top references
cited by
5
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      8
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

      Phagosome proteomes open the way to a better understanding of phagosome function

      review-article
      Author(s): 1 , , 2
      Publication date (Electronic):
      Journal: Genome Biology
      Publisher: BioMed Central

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Determination of the global protein composition of phagosomes is a first step to understanding how these organelles carry out their function.

          Abstract

          Phagocytic cells take up microbes and other particles into membrane-bounded organelles called phagosomes. Studies on the protein and lipid composition of model phagosomes containing latex beads are the first step in a systems-biology approach to understanding how these organelles function.

          Related collections

          Most cited references13

          • Record: found
          • Abstract: found
          • Article: not found

          The Phagosome Proteome

          Jérôme Garin, Roberto Diez, Sylvie Kieffer-Jaquinod … (2001)
          Phagosomes are key organelles for the innate ability of macrophages to participate in tissue remodeling, clear apoptotic cells, and restrict the spread of intracellular pathogens. To understand the functions of phagosomes, we initiated the systematic identification of their proteins. Using a proteomic approach, we identified >140 proteins associated with latex bead–containing phagosomes. Among these were hydrolases, proton pump ATPase subunits, and proteins of the fusion machinery, validating our approach. A series of unexpected proteins not previously described along the endocytic/phagocytic pathways were also identified, including the apoptotic proteins galectin3, Alix, and TRAIL, the anti-apoptotic protein 14-3-3, the lipid raft-enriched flotillin-1, the anti-microbial molecule lactadherin, and the small GTPase rab14. In addition, 24 spots from which the peptide masses could not be matched to entries in any database potentially represent new phagosomal proteins. The elaboration of a two-dimensional gel database of >160 identified spots allowed us to analyze how phagosome composition is modulated during phagolysosome biogenesis. Remarkably, during this process, hydrolases are not delivered in bulk to phagosomes, but are instead acquired sequentially. The systematic characterization of phagosome proteins provided new insights into phagosome functions and the protein or groups of proteins involved in and regulating these functions.
          Article 0 comments Cited 115 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus

            Lukas Huber (1994)
            We have examined the modifications occurring during the transformation of phagosomes into phagolysosomes in J-774 macrophages. The use of low density latex beads as markers of phagosomes (latex bead compartments, LBC) allowed the isolation of these organelles by flotation on a simple sucrose gradient. Two-dimensional gel electrophoresis, immunocytochemistry, and biochemical assays have been used to characterize the composition of LBC at different time points after their formation, as well as their interactions with the organelles of the endocytic pathway. Our results show that LBC acquire and lose various markers during their transformation into phagolysosomes. Among these are members of the rab family of small GTPases as well as proteins of the lamp family. The transfer of the LBC of lamp 2, a membrane protein associated with late endocytic structures, was shown to be microtubule dependent. Video-microscopy showed that newly formed phagosomes were involved in rapid multiple contacts with late components of the endocytic pathway. Collectively, these observations suggest that phagolysosome formation is a highly dynamic process that involves the gradual and regulated acquisition of markers from endocytic organelles.
            Article 0 comments Cited 104 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Selected lipids activate phagosome actin assembly and maturation resulting in killing of pathogenic mycobacteria.

              Anja Habermann, Raymond J. Moniz, Marian E. H. Bos … (2003)
              Pathogenic mycobacteria such as Mycobacterium tuberculosis and Mycobacterium avium facilitate disease by surviving intracellularly within a potentially hostile environment: the macrophage phagosome. They inhibit phagosome maturation processes, including fusion with lysosomes, acidification and, as shown here, membrane actin assembly. An in vitro assay developed for latex bead phagosomes (LBPs) provided insights into membrane signalling events that regulate phagosome actin assembly, a process linked to membrane fusion. Different lipids were found to stimulate or inhibit actin assembly by LBPs and mycobacterial phagosomes in vitro. In addition, selected lipids activated actin assembly and phagosome maturation in infected macrophages, resulting in a significant killing of M. tuberculosis and M. avium. In contrast, the polyunsaturated sigma-3 lipids behaved differently and stimulated pathogen growth. Thus, lipids can be involved in both stimulatory and inhibitory signalling networks in the phagosomal membrane.
              Article 0 comments Cited 73 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Genome Biol
                Title: Genome Biology
                Publisher: BioMed Central (London )
                ISSN (Print): 1465-6906
                ISSN (Electronic): 1465-6914
                Publication date (Print): 2007
                Publication date (Electronic): 15 March 2007
                Volume: 8
                Issue: 3
                Page: 207
                Affiliations
                [1 ]Cell Biology Program, EMBL, Meyerhofstrasse, 69117 Heidelberg, Germany
                [2 ]IHEM (U.N. Cuyo-CONICET), Casilla de Correo, Mendoza, 5500, Argentina
                Article
                Publisher ID: gb-2007-8-3-207
                DOI: 10.1186/gb-2007-8-3-207
                PMC ID: 1868947
                PubMed ID: 17367543
                SO-VID: 858143a7-a3c5-402e-8c89-ffdd65c1df0f
                Copyright © Copyright © 2007 BioMed Central Ltd
                History
                Categories
                Subject: Minireview

                ScienceOpen disciplines: Genetics
                Data availability:
                ScienceOpen disciplines: Genetics

                Comments

                Comment on this article

                scite_

                Similar content8

                See all similar

                Cited by5

                See all cited by

                Most referenced authors169

                See all reference authors