A glance at Listeria and Salmonella cell invasion: Different strategies to promote host actin polymerization

Silva, Cláudio Vieira da; Cruz, Leandro; Araújo, Núbia da Silva; Angeloni, Mariana Bodini; Fonseca, Belchiolina Beatriz; Gomes, Angélica de Oliveira; Carvalho, Fernando dos Reis; Gonçalves, Ana Lúcia Ribeiro; Barbosa, Bellisa de Freitas

doi:10.1016/j.ijmm.2011.05.003

Cited by 25 publications

(20 citation statements)

References 154 publications

(168 reference statements)

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“…According to Galan and Zhou [22] the Salmonella effector SipA binds to actin promoting a significant reduction in the concentration of its monomeric conformation. In addition, SipA increases the stability of actin bundles by modulating plastin actin-bundling activity [26]. Interestingly, we observed that L-plastin was more abundant in the beginning of infection and this result could consist in another evidence of SipA activity in MLN.…”

Section: Discussionmentioning

confidence: 52%

Proteomic analysis of porcine mesenteric lymph-nodes after Salmonella typhimurium infection

Martins¹,

Collado-Romero²,

Martínez-Gomáriz³

et al. 2012

Journal of Proteomics

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Section: Discussionmentioning

confidence: 52%

Proteomic analysis of porcine mesenteric lymph-nodes after Salmonella typhimurium infection

Martins¹,

Collado-Romero²,

Martínez-Gomáriz³

et al. 2012

Journal of Proteomics

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“…The best-characterized Salmonella invasion mechanism requires T3SS1 that initiates a process known as the "trigger" mechanism. It has been recently shown that Salmonella can also invade cells by a "zipper" entry process, typical of other pathogens like Listeria [12], through the Rck outer membrane protein, which induces a local accumulation of actin, leading to a discrete membrane alteration [13]. Another outer membrane protein, PagN, and the poreforming hemolysin HlyE also contribute to invasion by unknown mechanisms [14][15][16].…”

Section: Actin Cytoskeleton and Invasionmentioning

confidence: 99%

Impact ofSalmonella entericaType III Secretion System Effectors on the Eukaryotic Host Cell

Ramos‐Morales

2012

ISRN Cell Biology

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Type III secretion systems are molecular machines used by many Gram-negative bacterial pathogens to inject proteins, known as effectors, directly into eukaryotic host cells. These proteins manipulate host signal transduction pathways and cellular processes to the pathogen's advantage. Salmonella enterica possesses two virulence-related type III secretion systems that deliver more than forty effectors. This paper reviews our current knowledge about the functions, biochemical activities, host targets, and impact on host cells of these effectors. First, the concerted action of effectors at the cellular level in relevant aspects of the interaction between Salmonella and its hosts is analyzed. Then, particular issues that will drive research in the field in the near future are discussed. Finally, detailed information about each individual effector is provided.

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“…Well-characterized pathogens such as Listeria, Shigella, and Yersinia utilize host cell actin to enter cells (32)(33)(34)(35). Similarly, actin polymerization is important for rickettsial invasion of Drosophila and mammalian cells (6, 9); thus, the role of actin polymerization was examined for R. montanensis infection of tick cells.…”

Section: Resultsmentioning

confidence: 99%

Identification of Host Proteins Involved in Rickettsial Invasion of Tick Cells

et al. 2015

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Tick-borne spotted fever group (SFG) Rickettsia species are obligate intracellular bacteria capable of infecting both vertebrate and invertebrate host cells, an essential process for subsequent bacterial survival in distinct hosts. The host cell signaling molecules involved in the uptake of Rickettsia into mammalian and Drosophila cells have been identified; however, invasion into tick cells is understudied. Considering the movement of SFG Rickettsia between vertebrate and invertebrate hosts, the hypothesis is that conserved mechanisms are utilized for host cell invasion. The current study employed biochemical inhibition assays to determine the tick proteins involved in Rickettsia montanensis infection of tick-derived cells from a natural host, Dermacentor variabilis. The results revealed several tick proteins important for rickettsial invasion, including actin filaments, actin-related protein 2/3 complex, phosphatidylinositol-3=-kinase, protein tyrosine kinases (PTKs), Src family PTK, focal adhesion kinase, Rho GTPase Rac1, and neural Wiskott-Aldrich syndrome protein. Delineating the molecular mechanisms of rickettsial infection is critical to a thorough understanding of rickettsial transmission in tick populations and the ecology of tick-borne rickettsial diseases.T ick-borne rickettsial diseases caused by pathogenic bacteria belonging to the genera Rickettsia, Anaplasma, and Ehrlichia are steadily increasing in the United States (1). Infection associated with these obligate intracellular bacteria ranges from mild, self-limiting to severe, including death (2). In the typical transmission cycle, spotted fever group (SFG) rickettsiae transmit vertically during the tick life cycle stages and between vectors and vertebrate hosts during tick acquisition of a blood meal. In vertebrate hosts, mechanisms of SFG Rickettsia infection, including invasion, escape from the phagosome, intracellular growth, intracellular movement, and cell-to-cell spread, have been studied (3). Tick acquisition of SFG Rickettsia from rickettsemic hosts is poorly described, and despite the essential role for tick hosts in maintenance and transmission of SFG Rickettsia to vertebrate hosts, the biology of the tick cell-SFG Rickettsia interaction is understudied.The obligate intracellular nature of Rickettsia requires bacteria to invade both vertebrate and invertebrate host cells, and this process, host cell invasion by SFG Rickettsia, has been studied in mammalian and Drosophila cell lines. Mammalian ligands Ku70 and ␣ 2 ␤ 1 integrin interact with rickettsial outer membrane proteins B and A (OmpB and OmpA), respectively, and are involved in Rickettsia conorii invasion of mammalian host cells (4, 5). After binding to rickettsial OmpB, R. conorii induces signaling cascades in which Ku70 is initially ubiquitinated by c-Cbl ubiquitin ligase. Subsequently, signaling molecules, including Cdc42, protein tyrosine kinases (PTKs), phosphatidylinositol-3=-kinase (PI3-kinase), Src family tyrosine kinases (Src), focal adhesion kinase (FAK), and cortactin, c...

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A glance at Listeria and Salmonella cell invasion: Different strategies to promote host actin polymerization

Cited by 25 publications

References 154 publications

Proteomic analysis of porcine mesenteric lymph-nodes after Salmonella typhimurium infection

Proteomic analysis of porcine mesenteric lymph-nodes after Salmonella typhimurium infection

Impact ofSalmonella entericaType III Secretion System Effectors on the Eukaryotic Host Cell

Identification of Host Proteins Involved in Rickettsial Invasion of Tick Cells

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