Immunolocalization of Hsp60 in
            <i>Legionella pneumophila</i>

Garduño, Rafael A.; Faulkner, Gary; Trevors, Mary Ann; Vats, Neeraj; Hoffman, Paul S.

doi:10.1128/jb.180.3.505-513.1998

Cited by 105 publications

(50 citation statements)

References 54 publications

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“…However, as no other Cpn60 protein was tested this conclusion is still speculative. This Legionella Cpn60 protein is present on the bacterial surface and is also required for the invasion of the bacterium into non-phagocytic cells (Garduño et al, 1998a;Garduno, Garduno & Hoffman, 1998b).…”

Section: (1) Selected Moonlighting Actions Of Bacterial Cpn60 Proteinsmentioning

confidence: 99%

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

2013

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Chaperonin 60 is the prototypic molecular chaperone, an essential protein in eukaryotes and prokaryotes, whose sequence conservation provides an excellent basis for phylogenetic analysis. Escherichia coli chaperonin 60 (GroEL), the prototype of this family of proteins, has an established oligomeric-structure-based folding mechanism and a defined population of folding partners. However, there is a growing number of examples of chaperonin 60 proteins whose crystal structures and oligomeric composition are at variance with GroEL, suggesting that additional complexities in the protein-folding function of this protein should be expected. In addition, many organisms have multiple chaperonin 60 proteins, some of which have lost their protein-folding ability. It is emerging that this highly conserved protein has evolved a bewildering variety of additional biological functions - known as moonlighting functions - both within the cell and in the extracellular milieu. Indeed, in some organisms, it is these moonlighting functions that have been left after the loss of the protein-folding activity. This highlights the major paradox in the biology of chaperonin 60. This article reviews the relationship between the folding and non-folding (moonlighting) activities of the chaperonin 60 family and discusses current knowledge on their molecular evolution focusing on protein domains involved in the non-folding chaperonin functions in an attempt to understand the emerging biology of this evolutionarily ancient protein family.

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Section: (1) Selected Moonlighting Actions Of Bacterial Cpn60 Proteinsmentioning

confidence: 99%

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

2013

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“…GroEL is present on the surface of H. pylori as a result of a non-specific absorption process (Phadnis et al 1996). In contrast, it is specifically transported to the surface of Legionella pneumophila and its surface location does not require autolysis of vegetative cells (Garduño et al 1998). A role for surface-associated GroEL in pathogenicity has been postulated (Dunn et al 1997).…”

Section: Other Proteins In the Exosporiummentioning

confidence: 99%

Characterization of the exosporium of Bacillus cereus

Charlton

Moir

Baillie³

1999

J Appl Microbiol

112

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Exosporium components from endospores of Bacillus cereus ATCC 10876 were purified and separated by gel electrophoresis. Several of the proteins for which N‐terminal sequences were recovered were found to have homologues in protein databases which have been demonstrated to have enzymic activity in other organisms. Amongst these is a zinc metalloprotease, immune inhibitor A, already described in B. thuringiensis. This has been shown to be present in an active 73 kDa form on the exosporium of B. cereus. Other proteins associated with the exosporium include the molecular chaperone GroEL and a homologue of RocA (1‐pyrroline‐5‐carboxylate dehydrogenase (EC 1.5.1.12)) of B. subtilis. Although these are unlikely to represent integral structural proteins of the exosporium, the observation that they are selectively present in the spore surface layer suggests that this layer may have functional significance.

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“…Upon entry into the post-exponential growth phase, L. pneumophila undergoes dramatic phenotypic and morphological changes and exhibits several virulence traits, including motility, stress resistance, pore-forming activity, and the ability to evade endocytic fusion and replicate intracellularly (Byrne and Swanson, 1998;Garduno et al, 1998;Alli et al, 2000;Garduno et al, 2002;Molmeret et al, 2002a;Hiltz et al, 2004). Whether other species of Legionella exhibit similar growth phase-dependent trigger of virulence traits is not known.…”

Section: Introductionmentioning

confidence: 99%

Early trafficking and intracellular replication of Legionella longbeachaea within an ER-derived late endosome-like phagosome

Asare¹,

Kwaik²

2007

Cell Microbiol

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SummaryLegionella pneumophila is the predominant cause of Legionnaires' disease in the USA and Europe in contrast to Legionella longbeachaea, which is the leading cause of the disease in Western Australia. The ability of L. pneumophila to replicate intracellularly is triggered at the post-exponential phase along with expression of other virulence traits, such as motility. We show that while motility of L. longbeachaea is triggered upon growth transition into postexponential phase, its ability to proliferate intracellularly is totally independent of the bacterial growth phase. Within macrophages, L. pneumophila replicates in a phagosome that excludes early and late endocytic markers and is surrounded by the rough endoplasmic reticulum (RER). In contrast, the L. longbeachaea phagosome colocalizes with the early endosomal marker early endosomal antigen 1 (EEA1) and the late endosomal markers lysosomal associated membrane glycoprotein 2 (LAMP-2) and mannose 6-phosphate receptor (M6PR), and is surrounded by the RER. The L. longbeachaea phagosome does not colocalize with the vacuolar ATPase (vATPase) proton pump, and the lysosomal luminal protease Cathepsin D, or the lysosomal tracer Texas red Ovalbumin (TROV). Intracellular proliferation of L. longbeachaea occurs in LAMP-2-positive phagosomes that are remodelled by the RER. Despite their distinct trafficking, both L. longbeachaea and L. pneumophila can replicate in communal phagosomes whose biogenesis is predominantly modulated by L. longbeachaea into LAMP-2-positive phagosomes. In addition, the L. pneumophila dotA mutant is rescued for intracellular replication if it co-inhabits the phagosome with L. longbeachaea. During late stages of infection, L. longbeachaea escape into the cytoplasm, prior to lysis of the macrophage, similar to L. pneumophila. We conclude that the L. longbeachaea phagosome matures to a non-acidified late endosome-like stage that is remodelled by the RER, indicating an idiosyncratic trafficking of L. longbeachaea compared with other intracellular pathogens, and a divergence in its intracellular lifestyle from L. pneumophila. In addition, re-routing biogenesis of the L. pneumophila phagosome into a late endosome controlled by L. longbeachaea has no effect on intracellular replication.

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Immunolocalization of Hsp60 in Legionella pneumophila

Cited by 105 publications

References 54 publications

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

Characterization of the exosporium of Bacillus cereus

Early trafficking and intracellular replication of Legionella longbeachaea within an ER-derived late endosome-like phagosome

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