Bacterial pathogenesis: exploiting cellular adherence

Boyle, Erin C.; Finlay, B. Brett

doi:10.1016/s0955-0674(03)00099-1

Cited by 124 publications

(86 citation statements)

References 54 publications

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“…Because Src also controls cell invasion by yersiniae, we used cytochalasin D to assess the role of bacterial internalization on autophagy induction. Cytochalasin D depolymerizes F-actin and thereby prevents bacterial cell invasion (58,59,61). This drug similarly inhibited the conversion of LC3-II triggered by WA-C and WA-⌬lcrD (Fig.…”

Section: Yersinia-induced Autophagy Involves Engagement Of ␤ 1 Integrmentioning

confidence: 79%

“…Yersiniae deficient in the secretion of Yops efficiently activated autophagy through the engagement of ␤ 1 integrin receptors and cell invasion. The induction of autophagy involved the Yersinia adhesins invasin and YadA which cluster ␤ 1 integrins to gain access into eukaryotic cells (26,27,58). Many bacteria and viruses stimulate ␤ 1 integrins (75)(76)(77), and this is a first study demonstrating the induction of autophagy as a result of microbial ␤ 1 integrin activation.…”

Section: Discussionmentioning

confidence: 99%

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β1 Integrin-Dependent Engulfment of Yersinia enterocolitica by Macrophages Is Coupled to the Activation of Autophagy and Suppressed by Type III Protein Secretion

Deuretzbacher

Czymmeck

Reimer

et al. 2009

The Journal of Immunology

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Autophagy is a central lysosomal degradation process that is essential for the maintenance of cellular homeostasis. Autophagy has furthermore emerged as integral part of the host immune response. Autophagic processes promote the separation and degradation of intracellular microorganisms which contributes to the development of innate and adaptive immunity. Some pathogenic microbes have therefore evolved mechanisms to evade or impede autophagy. We analyzed the effects of the enteropathogenic bacterium Yersinia enterocolitica on autophagy in macrophages. Yersiniae use a number of defined adhesins and secreted proteins to manipulate host immune responses. Our results showed that Y. enterocolitica defective in type III protein secretion efficiently activated autophagy in macrophages. Autophagy was mediated by the Yersinia adhesins invasin and YadA and particularly depended on the engagement of β1 integrin receptors. Several autophagy-related events followed β1 integrin-mediated engulfment of the bacteria including the formation of autophagosomes, processing of the marker protein LC3, redistribution of GFP-LC3 to bacteria-containing vacuoles, and the segregation of intracellular bacteria by autophagosomal compartments. These results provide direct evidence for the linkage of β1 integrin-mediated phagocytosis and autophagy induction. Multiple microbes signal through integrin receptors, and our results suggest a general principle by which the sensing of an extracellular microbe triggers autophagy. Owing to the importance of autophagy as host defense response, wild-type Y. enterocolitica suppressed autophagy by mobilizing type III protein secretion. The subversion of autophagy may be part of the Y. enterocolitica virulence strategy that supports bacterial survival when β1 integrin-dependent internalization and autophagy activation by macrophages are deleterious for the pathogen.

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Section: Yersinia-induced Autophagy Involves Engagement Of ␤ 1 Integrmentioning

confidence: 79%

Section: Discussionmentioning

confidence: 99%

β1 Integrin-Dependent Engulfment of Yersinia enterocolitica by Macrophages Is Coupled to the Activation of Autophagy and Suppressed by Type III Protein Secretion

Deuretzbacher

Czymmeck

Reimer

et al. 2009

The Journal of Immunology

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“…For decades, microbial virulence has been linked primarily to factors such as microbial adherence (28), invasion (29,30), toxin production (31, 32), or iron-chelating capacity (33) (34).…”

Section: Discussionmentioning

confidence: 99%

Attenuated virulence of aFrancisellamutant lacking the lipid A 4′-phosphatase

Wang¹,

Ribeiro²,

Guan³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

117

161

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Francisella tularensis causes tularemia, a highly contagious disease of animals and humans, but the virulence features of F. tularensis are poorly defined. F. tularensis and the related mouse pathogen Francisella novicida synthesize unusual lipid A molecules lacking the 4-monophosphate group typically found in the lipid A of Gram-negative bacteria. LpxF, a selective phosphatase located on the periplasmic surface of the inner membrane, removes the 4-phosphate moiety in the late stages of F. novicida lipid A assembly. To evaluate the relevance of the 4-phosphatase to pathogenesis, we constructed a deletion mutant of lpxF and compared its virulence with wild-type F. novicida. Intradermal injection of 10 6 wild-type but not 10 8 mutant F. novicida cells is lethal to mice. The rapid clearance of the lpxF mutant is associated with a stronger local cytokine response and a greater influx of neutrophils compared with wild-type. The F. novicida mutant was highly susceptible to the cationic antimicrobial peptide polymyxin. LpxF therefore represents a kind of virulence factor that confers a distinct lipid A phenotype, preventing Francisella from activating the host innate immune response and preventing the bactericidal actions of cationic peptides. Francisella lpxF mutants may be useful for immunization against tularemia.antimicrobial peptides ͉ outer membrane ͉ innate immunity ͉ polymyxin ͉ tularemia G ram-negative bacteria contain an asymmetric outer membrane with glycerophospholipids on the inside and lipid A (Fig.

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“…Indeed, one cadherin (MBCDH1) has been shown to localize to the microvillar collar of M. brevicollis (1). Furthermore, there is precedent for a physiologically important interaction between bacteria and cadherins in metazoans: Some pathogenic bacteria interact with classical cadherins in gut epithelia, thereby stimulating the host cells to phagocytose the invading pathogen (55)(56)(57).…”

Section: Radiation Of Cadherins In Choanoflagellate and Metazoan Linementioning

confidence: 99%

Origin of metazoan cadherin diversity and the antiquity of the classical cadherin/β-catenin complex

Nichols

Roberts

Richter

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

170

196

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The evolution of cadherins, which are essential for metazoan multicellularity and restricted to metazoans and their closest relatives, has special relevance for understanding metazoan origins. To reconstruct the ancestry and evolution of cadherin gene families, we analyzed the genomes of the choanoflagellate Salpingoeca rosetta, the unicellular outgroup of choanoflagellates and metazoans Capsaspora owczarzaki, and a draft genome assembly from the homoscleromorph sponge Oscarella carmela. Our finding of a cadherin gene in C. owczarzaki reveals that cadherins predate the divergence of the C. owczarzaki, choanoflagellate, and metazoan lineages. Data from these analyses also suggest that the last common ancestor of metazoans and choanoflagellates contained representatives of at least three cadherin families, lefftyrin, coherin, and hedgling. Additionally, we find that an O. carmela classical cadherin has predicted structural features that, in bilaterian classical cadherins, facilitate binding to the cytoplasmic protein β-catenin and, thereby, promote cadherin-mediated cell adhesion. In contrast with premetazoan cadherin families (i.e., those conserved between choanoflagellates and metazoans), the later appearance of classical cadherins coincides with metazoan origins.

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Bacterial pathogenesis: exploiting cellular adherence

Cited by 124 publications

References 54 publications

β1 Integrin-Dependent Engulfment of Yersinia enterocolitica by Macrophages Is Coupled to the Activation of Autophagy and Suppressed by Type III Protein Secretion

β1 Integrin-Dependent Engulfment of Yersinia enterocolitica by Macrophages Is Coupled to the Activation of Autophagy and Suppressed by Type III Protein Secretion

Attenuated virulence of aFrancisellamutant lacking the lipid A 4′-phosphatase

Origin of metazoan cadherin diversity and the antiquity of the classical cadherin/β-catenin complex

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