Cellular Microbiology Journal Impact Factor & Information

Publisher: Wiley

Journal description

Cellular Microbiology publishes the best original scientific contribution of the intersection of microbial on host-cell biology. The focus is the host cell responses elicited by the interaction of micro-organisms. Equal emphasis is placed on responses to prokaryotic, viral and eukaryotic micro-organisms. In addition to mammalion systems, papers addressing other hosts such as plants and insects are strongly encourage. Exploitation of host cell structure; Modification of cell signalling pathways; Molecular responses of the host cell; Responses of tissues and whole organs; Systemic effects elicited by micro-organisms; Induction of immune response; Modulation and exploitation of immune response; Remodelling of tissues; Co-pathogen interactions.

Current impact factor: 4.82

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 4.816
2012 Impact Factor 4.811
2011 Impact Factor 5.458
2010 Impact Factor 5.625
2009 Impact Factor 5.725
2008 Impact Factor 5.598
2007 Impact Factor 5.293
2006 Impact Factor 5.07
2005 Impact Factor 6.333
2004 Impact Factor 6.097
2003 Impact Factor 5.336
2002 Impact Factor 4.895
2001 Impact Factor 4.557
2000 Impact Factor 3.409

Impact factor over time

Impact factor
Year

Additional details

5-year impact 5.09
Cited half-life 5.30
Immediacy index 1.31
Eigenfactor 0.03
Article influence 1.85
Website Cellular Microbiology website
Other titles Cellular microbiology (Online)
ISSN 1462-5822
OCLC 42869627
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Wiley

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 12 months embargo
  • Conditions
    • Some journals have separate policies, please check with each journal directly
    • On author's personal website, institutional repositories, arXiv, AgEcon, PhilPapers, PubMed Central, RePEc or Social Science Research Network
    • Author's pre-print may not be updated with Publisher's Version/PDF
    • Author's pre-print must acknowledge acceptance for publication
    • On a non-profit server
    • Publisher's version/PDF cannot be used
    • Publisher source must be acknowledged with citation
    • Must link to publisher version with set statement (see policy)
    • If OnlineOpen is available, BBSRC, EPSRC, MRC, NERC and STFC authors, may self-archive after 12 months
    • If OnlineOpen is available, AHRC and ESRC authors, may self-archive after 24 months
    • Publisher last contacted on 07/08/2014
    • This policy is an exception to the default policies of 'Wiley'
  • Classification
    ​ yellow

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Salmonella invades epithelial cells and survives within a membrane-bound compartment, the Salmonella-Containing Vacuole (SCV). We isolated and determined the host protein composition of the SCV at 30 minutes and 3 hours of infection to identify and characterize novel regulators of intracellular bacterial localization and growth. Quantitation of the SCV protein content revealed 392 host proteins specifically enriched at SCVs, out of which 173 associated exclusively with early SCVs, 124 with maturing SCV, and 95 proteins during both time-points. Vacuole interactions with endoplasmic reticulum-derived COPII vesicles modulate early steps of SCV maturation, promoting SCV rupture and bacterial hyper-replication within the host cytosol. On the other hand, SCV interactions with VAMP7-positive lysosome-like vesicles promote Salmonella-induced filament formation and bacterial growth within the late SCV. Our results reveal that the dynamic communication between the SCV and distinct host organelles affects both intracellular Salmonella localization and growth at successive steps of host cell invasion. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12475
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    ABSTRACT: The human pathogen Helicobacter pylori colonises half of the global population. Residing at the stomach epithelium, it contributes to the development of diseases like gastritis, duodenal and gastric ulcers, and gastric cancer. A major factor is the secreted vacuolating toxin VacA, which forms anion-selective channels in the endosome membrane that cause the compartment to swell, but the composition and purpose of the resulting VacA-containing vacuoles (VCVs) is still unknown. VacA exerts influence on the host immune response in various ways, including inhibition of T-cell activation and proliferation and suppression of the host immune response. In this study, for the first time the composition of VCVs from T-cells was comprehensively analysed to investigate VCV function. VCVs were successfully isolated via immunomagnetic separation and the purified vacuoles were analysed by mass spectrometry. We detected a set of 122 VCV-specific proteins, implicated amongst others in immune response, cell death and cellular signalling processes, all of which VacA is known to influence. One of the individual proteins studied further was stromal interaction molecule (STIM1), a calcium sensor residing in the endoplasmic reticulum (ER) important in store-operated calcium entry (SOCE). Live cell imaging microscopy data demonstrated co-localisation of VacA with STIM1 in the ER and indicated that VacA may interfere with the movement of STIM1 towards the plasma membrane-localised calcium release activated calcium (CRAC) channel protein ORAI1 in response to Ca(2+) store depletion. Furthermore, VacA inhibited the increase of cytosolic free Ca(2+) in the Jurkat E6-1 T-cell line and human CD4(+) T cells. The presence of VacA in the ER and its trafficking to the Golgi apparatus was confirmed in HeLa cells, identifying these two cellular compartments as novel VacA target structures. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12474
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    ABSTRACT: Coxsackievirus infection can lead to viral myocarditis and its sequela, dilated cardiomyopathy, which represent major causes of cardiovascular mortality worldwide in children. Yet, the host genetic susceptible factors and the underlying mechanisms by which viral infection damages cardiac function remain to be fully resolved. Dysferlin is a transmembrane protein highly expressed in skeletal and cardiac muscles. In humans, mutations in the dysferlin gene can cause limb-girdle muscular dystrophy type 2B and Miyoshi myopathy. Dysferlin-deficiency has also been linked to cardiomyopathy. Defective muscle membrane repair has been suggested to be an important mechanism responsible for muscle degeneration in dysferlin-deficient patients and animals. Using both naturally occurring and genetically engineered dysferlin-deficient mice, we demonstrated that loss of dysferlin confers increased susceptibility to coxsackievirus infection and myocardial damage. More interestingly, we found that dysferlin is cleaved following coxsackieviral infection through the proteolytic activity of virally encoded proteinases, suggesting an important mechanism underlying virus-induced cardiac dysfunction. Our results in this study not only identify dysferlin-deficiency as a novel host risk factor for viral myocarditis but also reveal a key mechanism by which coxsackievirus infection impairs cardiac function, leading to the development of dilated cardiomyopathy. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12473
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    ABSTRACT: Collective evidence argues that two members of the Nucleo-cytoplasmic large DNA viruses (NCLDVs) acquire their membrane from open membrane intermediates, postulated to be derived from membrane rupture. We now study membrane acquisition of the NCLDV African swine fever virus (ASFV). By electron tomography (ET) the virion assembles a single bilayer derived open membrane precursors that collect as ribbons in the cytoplasm. Biochemically, lumenal ER proteins are released into the cytosol, arguing that the open intermediates are ruptured ER membranes. ET shows that viral capsid assembles on the convex side of the open viral membrane to shape it into an icosahedron. The viral capsid is composed of tiny spikes with a diameter of ∼5 nm, connected to the membrane by a 6 nm wide structure displaying thin striations, as observed by several complementary EM imaging methods. Immature particles display an opening that closes after uptake of the viral genome and core proteins, followed by the formation of the mature virion. Together with our previous data this study shows a common principle of NCLDVs to build a single internal envelope from open membrane intermediates. Our data now provide biochemical evidence that these open intermediates result from rupture of a cellular membrane, the ER. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12468
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    ABSTRACT: Upon infection of epithelial cells, enteropathogenic E. coli (EPEC) suppresses host cell inflammatory signaling in a type III secretion system (T3SS) dependent manner. Two key T3SS effector proteins involved in this response are NleE and NleC. NleC is a zinc metalloprotease effector that degrades the p65 subunit of NF-κB. Although site of p65 cleavage by NleC is now well-described, other areas of interaction have not been precisely defined. Here we constructed overlapping truncations of p65 to identify regions required for NleC cleavage. We determined that NleC cleaved both p65 and p50 within the Rel homology domain (RHD) and that two motifs, E22 IIE25 and P177 VLS180 , within the RHD of p65 were important for recognition and binding by NleC. Alanine substitution of one or both of these motifs protected p65 from binding and degradation by NleC. The E22 IIE25 and P177 VLS180 motifs were located within the structurally distinct N-terminal subdomain of the RHD involved in DNA binding by p65 on adjacent, parallel strands. Although these motifs have not been recognised previously, both were needed for the correct localization and function of p65. In summary, this work has identified two regions of p65 within the RHD needed for binding and cleavage by NleC and provides further insight into the molecular basis of substrate recognition by a T3SS effector. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12469
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    ABSTRACT: The pathogenic amoeba, Entamoeba histolytica is one of the causative agents of health hazards in tropical countries. It causes amoebic dysentery, colitis and liver abscesses in human. Iron is one of the essential nutritional resources for survival and chronic infection caused by the amoeba. The parasite has developed multiple ways to import, sequester and utilize iron from various iron binding proteins from its host. In spite of its central role in pathogenesis, the mechanism of iron uptake by the parasite is largely unknown. Here, we carried out a systematic study to understand the role of some of the amoebic homologues of mammalian endocytic Rab GTPases (Rab5 and Rab21, Rab7A and Rab7B) in intracellular transport of human holo-transferrin by the parasite. Flow cytometry and quantitative microscopic image analysis revealed that Rab5 and Rab7A are required for the biogenesis of amoebic giant endocytic vacuoles and regulate the early phase of intracellular trafficking of transferrin. Rab7B is involved in the late phase, leading to the degradation of transferrin in the amoebic lysosome like compartments. Using time lapsed fluorescence imaging in fixed trophozoites, we determined the kinetics of the vesicular transport of transferrin through Rab5, Rab7A and Rab7B positive compartments. The involvement of Rab7A in the early phase of endocytosis by the parasite marks a significant divergence from its host in terms of spatio-temporal regulation by the Rab GTPases. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12470
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    ABSTRACT: The epigenetics of host-pathogen interactions is emerging as an interesting angle from which to study how parasites have evolved sophisticated strategies to manipulate host gene transcription and protein expression. In this review we discuss the application of an operational framework to investigate the host cell signalling pathways that are induced by intracellular parasites and the epigenomic consequences in the host nucleus. To illustrate this conceptual approach, we have focused on examples from two eukaryotic intracellular parasites of the apicomplexa phylum: Theileria and Toxoplasma. We review recent findings on intracellular parasitism strategies for hijacking host nuclear functions and discuss how we might think of the parasite and its proteome as an intracellular epigenator. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12471
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    ABSTRACT: SUMOylation is an important post-translational modification conserved in eukaryotic organisms. In Trypanosoma brucei, SUMO is essential in procyclic and bloodstream forms. Furthermore, SUMO has been linked to the antigenic variation process, as a highly SUMOylated focus was recently identified within chromatin-associated proteins of the active VSG expression site. We aimed to establish a reliable strategy to identify SUMO conjugates in T. brucei. We expressed various tagged variants of SUMO from the endogenous locus. His-HA-TbSUMO was useful to validate the tag functionality but SUMO conjugates were not enriched enough over contaminants after affinity purification. A Lys-deficient SUMO version, created to reduce contaminants by Lys-C digestion, was able to overcome this issue but did not allow mapping many SUMOylation sites. This cell line was in turn useful to demonstrate that polySUMO chains are not essential for parasite viability. Finally, a His-HA-TbSUMO(T106K) version allowed the purification of SUMO conjugates and, after digestion with Lys-C, the enrichment for diGly-Lys peptides using specific antibodies. This site specific proteomic strategy led us to identify 45 SUMOylated proteins and 53 acceptor sites unambiguously. SUMOylated proteins belong mainly to nuclear processes such as DNA replication and repair, transcription, rRNA biogenesis, and chromatin remodelling, among others. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12467
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    ABSTRACT: Klebsiella pneumoniae is an important cause of community-acquired and nosocomial pneumonia. Evidence indicates that Klebsiella might be able to persist intracellularly within a vacuolar compartment. This study was designed to investigate the interaction between Klebsiella and macrophages. Engulfment of K. pneumoniae was dependent on host cytoskeleton, cell plasma membrane lipid rafts and the activation of PI 3-kinase (PI3K). Microscopy studies revealed that K. pneumoniae resides within a vacuolar compartment, the Klebsiella containing vacuolae (KCV), which traffics within vacuoles associated with the endocytic pathway. In contrast to UV-killed bacteria, the majority of live bacteria did not colocalize with markers of the lysosomal compartment. Our data suggest that K. pneumoniae triggers a programmed cell death in macrophages displaying features of apoptosis. Our efforts to identify the mechanism(s) whereby K. pneumoniae prevents the fusion of the lysosomes to the KCV uncovered the central role of the PI3K-Akt-Rab14 axis to control the phagosome maturation. Our data revealed that the capsule is dispensable for Klebsiella intracellular survival if bacteria were not opsonized. Furthermore, the environment found by Klebsiella within the KCV triggered the downregulation of the expression of cps. Altogether, this study proves evidence that K. pneumoniae survives killing by macrophages by manipulating phagosome maturation which may contribute to Klebsiella pathogenesis. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12466
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    ABSTRACT: Toll like receptor (TLR) mediated interactions of Mycobacterium tuberculosis (M. tb) with macrophages are a major determinant in the outcome of innate immune defence and the subsequent adaptive immune responses. Here we report a novel interaction of the M. tb protein pair PE9 (Rv1088)-PE10 (Rv1089) with the macrophage TLR4 leading to apoptosis and modulation of cytokine levels. We demonstrate that the two proteins physically interact and that PE9 is required for the cell wall localization of PE10 in Mycobacterium smegmatis. Interaction of the PE9-PE10 complex with TLR4 in THP-1 macrophages was associated with increased levels of phospho-IRF3 which correlated with an increase in transcript levels of its target gene IFN-β. THP-1 macrophages treated with the PE9-PE10 complex showed multiple hallmarks of apoptosis and modulation of IL-1b and IL-10 levels. All these effects were abrogated when cells were treated either with an antibody to PE10 or an anti-TLR4 antibody, indicating that the complex specifically interacts with TLR4 through PE10, establishing this protein pair as a TLR4 ligand. This novel observation of two PE proteins forming functional hetero-dimers represents a considerable expansion of the PE_PPE repertoire in the context of receptor engagement and the concomitant modulation of host responses by this unique class of proteins. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12462
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    ABSTRACT: The modulation of the chromatin organization of eukaryotic cells plays an important role in regulating key cellular processes including host defence mechanisms against pathogens. Thus, to successfully survive in a host cell, a sophisticated bacterial strategy is the subversion of nuclear processes of the eukaryotic cell. Indeed, the number of bacterial proteins that target host chromatin to remodel the host epigenetic machinery is expanding. Some of the identified bacterial effectors that target the chromatin machinery are "eukaryotic-like" proteins as they mimic eukaryotic histone writers in carrying the same enzymatic activities. The best-studied examples are the SET-domain proteins that methylate histones to change the chromatin landscape. In this review we will discuss SET-domain proteins identified in the Legionella, Chlamydia and Bacillus genomes that encode enzymatic activities targeting host histones. Moreover, we discuss their possible origin as having evolved from prokaryotic ancestors or having been acquired from their eukaryotic hosts during their co-evolution. The characterization of such bacterial effectors as modifiers of the host chromatin landscape is an exciting field of research as it elucidates new bacterial strategies to manipulate host functions through histone modifications but it also may identify new modifications of the mammalian host cells not known before. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12463
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    ABSTRACT: In recent years, understanding of the nucleolus has undergone a renaissance. Once considered primarily as the sites of ribosome biogenesis, nucleoli are now understood to be highly dynamic, multifunctional structures that participate in a plethora of cellular functions including regulation of the cell cycle, SRP assembly, apoptosis, and stress responses. Although the molecular/mechanistic details of many of these functions remain only partially resolved, it is becoming increasingly apparent that nucleoli are also common targets of almost all types of viruses, potentially allowing viruses to manipulate cellular responses and the intracellular environment to facilitate replication and propagation. Importantly, a number of recent studies have moved beyond early descriptive observations to identify key roles for nucleolar interactions in the viral life cycle and pathogenesis. While it is perhaps unsurprising that many viruses that replicate within the nucleus also form interactions with nucleoli, the roles of nucleoli in the biology of cytoplasmic viruses is less intuitive. Nevertheless, a number of positive stranded RNA viruses that replicate exclusively in the cytoplasm are known to express proteins that enter the nucleus and target nucleoli, and recent data have indicated similar processes in several cytoplasmic negative sense RNA viruses. Here, we review this emerging aspect of the virus-host interface with a focus on examples where virus-nucleolus interactions have been linked to specific functional outcomes/mechanistic processes in infection, and on the nucleolar interfaces formed by viruses that replicate exclusively in the cytoplasm. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 06/2015; DOI:10.1111/cmi.12465
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    ABSTRACT: Porphyromonas gingivalis is a prominent periodontal, and emerging systemic, pathogen that redirects host cell signaling pathways and modulates innate immune responses. In this study we show that P. gingivalis infection induces the dephosphorylation and activation of FOXO1, 3, and 4 in gingival epithelial cells. In addition, immunofluorescence showed that FOXO1 accumulated in the nucleus of P. gingivalis-infected cells. Quantitative RT-PCR (qRT-PCR) demonstrated that transcription of genes involved in protection against oxidative stress (Cat, Sod2, Prdx3), inflammatory responses (IL1β), and anti-apoptosis (Bcl-6) was induced by P. gingivalis, and siRNA-mediated knockdown of FOXO1 suppressed the transcriptional activation of these genes. P. gingivalis-induced secretion of IL-1β and inhibition of apoptosis were also inhibited by FOXO1 knockdown. Neutralization of reactive oxygen species (ROS) by N-acetyl-l-cysteine (NAC) blocked the activation of FOXO1 by P. gingivalis and concomitantly suppressed the activation of oxidative stress responses, anti-apoptosis programs and IL-β production. Inhibition of JNK either pharmacologically or by siRNA, reduced FOXO1 activation and downstream FOXO1-dependent gene regulation in response to P. gingivalis. The results indicate P. gingivalis induced ROS activate FOXO transcription factors through JNK signaling, and that FOXO1 controls oxidative stress responses, inflammatory cytokine production and cell survival. These data position FOXO as an important signaling node in the epithelial cell-P. gingivalis interaction, with particular relevance to cell fate and dysbiotic host responses. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 05/2015; DOI:10.1111/cmi.12459
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    ABSTRACT: The matrix protein 1 (M1) is the most abundant structural protein in influenza A virus particles. It oligomerizes to form the matrix layer under the lipid membrane, sustaining stabilization of the morphology of the virion. The present study indicates M1 forms oligomers based on a four-fold symmetrical oligomerization pattern. Further analysis revealed that the oligomerization pattern of M1 was controlled by a highly conserved region within the C-terminal domain. Two polar residues of this region, serine-183 (S183) and Threonine-185 (T185), were identified to be critical for the oligomerization pattern of M1. M1 point mutants suggest that single S183A or T185A substitution could result in the production of morphologically filamentous particles, while double substitutions, M1-S183A/T185A, totally disrupted the four-fold symmetry and resulted in the failure of virus production. These data indicate that the polar groups in these residues are essential to control the oligomerization pattern of M1. Thus, the present study will aid in determining the mechanisms of influenza A virus matrix layer formation during virus morphogenesis. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 05/2015; DOI:10.1111/cmi.12457
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    ABSTRACT: Control of host epigenetics is becoming evident as a mechanism by which symbionts and pathogens survive. Anaplasma phagocytophilum, an obligate intracellular bacterium, downregulates multiple host defense genes where histone deacetylase 1 (HDAC1) binds and histone 3 is deacetylated at their promoters, including the NADPH oxidase component, CYBB. How HDAC1 is targeted to defense gene promoters is unknown. Ankyrin A (AnkA), an A. phagocytophilum T4SS effector, enters the granulocyte nucleus, binds stretches of AT-rich DNA and alters transcription of antimicrobial defense genes, including downregulation of CYBB. Here we found AnkA binds to a predicted matrix attachment region in the proximal CYBB promoter. Using the CYBB promoter as a model of cis-gene silencing, we interrogated the mechanism of AnkA-mediated CYBB repression. The N-terminus of AnkA was critical for nuclear localization, the central ANK repeats and C-terminus were important for DNA binding, and most promoter activity localized to the central ANK repeats. Furthermore, a direct interaction between AnkA and HDAC1 was detected at the CYBB promoter, and was critical for AnkA-mediated CYBB repression. This novel microbial manipulation of host chromatin and gene expression provides important evidence of the direct effects that prokaryotic nuclear effectors can exert over host transcription and function. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 05/2015; DOI:10.1111/cmi.12461