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: 4.92

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 4.915
2013 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

Additional details

5-year impact 4.88
Cited half-life 6.40
Immediacy index 1.28
Eigenfactor 0.02
Article influence 1.76
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


  • 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
    • Non-Commercial
    • 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

  • Timothy C Barnett · Jason N Cole · Tania Rivera-Hernandez · Anna Henningham · James C Paton · Victor Nizet · Mark J Walker
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    ABSTRACT: Group A Streptococcus (Streptococcus pyogenes; GAS), group B Streptococcus (Streptococcus agalactiae; GBS) and Streptococcus pneumoniae (pneumococcus) are host-adapted bacterial pathogens among the leading infectious causes of human morbidity and mortality. These microbes and related members of the genus Streptococcus produce an array of toxins that act against human cells or tissues, resulting in impaired immune responses and subversion of host physiological processes to benefit the invading microorganism. This toxin repertoire includes hemolysins, proteases, superantigens and other agents that ultimately enhance colonization and survival within the host and promote dissemination of the pathogen. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 10/2015; DOI:10.1111/cmi.12531
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    ABSTRACT: The human-adapted organism Neisseria gonorrhoeae is the causative agent of gonorrhea a sexually transmitted infection. It readily colonizes the genital, rectal, and nasalpharyngal mucosa during infection. While it is well-established that N. gonorrhoeae recruits and modulates the functions of polymorphonuclear leukocytes (PMNs) during infection, how N. gonorrhoeae interacts with macrophages present in infected tissue is not fully defined. We studied the interactions of N. gonorrhoeae with two human monocytic cell lines, THP-1 and U937, and primary monocytes, all differentiated into macrophages. Most engulfed bacteria were killed in the phagolysosome, but a subset of bacteria were able to survive and replicate inside the macrophages suggesting that those cells may be an unexplored cellular reservoir for N. gonorrhoeae during infection. N. gonorrhoeae was able to modulate macrophage apoptosis, N. gonorrhoeae induced apoptosis in THP-1 cells whereas it inhibited induced apoptosis in U937 cells and primary human macrophages. Furthermore, N. gonorrhoeae induced expression of inflammatory cytokines in macrophages, suggesting a role for macrophages in recruiting PMNs to the site of infection. These results indicate macrophages may serve as a significant replicative niche for N. gonorrhoeae and play an important role in gonorrheal pathogenesis. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 10/2015; DOI:10.1111/cmi.12529
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    ABSTRACT: Neutrophils store large quantities of neutrophil serine proteases (NSPs) that contribute, via multiple mechanisms, to antibacterial immune defenses. Even though neutrophils are indispensable in fighting Staphylococcus aureus infections, the importance of NSPs in anti-staphylococcal defense is yet unknown. However, the fact that S. aureus produces three highly specific inhibitors for NSPs (the extracellular adherence proteins (EAPs) Eap, EapH1 and EapH2), suggest that these proteases are important for host defenses against this bacterium. In this study we demonstrate that NSPs can inactivate secreted virulence factors of S. aureus and that EAP proteins function to prevent this degradation. Specifically, we find that a large group of S. aureus immune-evasion proteins is vulnerable to proteolytic inactivation by NSPs. In most cases, NSP cleavage leads to functional inactivation of virulence proteins. Interestingly, proteins with similar immune-escape functions appeared to have differential cleavage sensitivity towards NSPs. Using targeted mutagenesis and complementation analyses in S. aureus, we demonstrate that all EAP proteins can protect other virulence factors from NSP degradation in complex bacterial supernatants. These findings show that NSPs inactivate S. aureus virulence factors. Moreover, the protection by EAP proteins can explain why this antibacterial function of NSPs was masked in previous studies. Furthermore, our results indicate that therapeutic inactivation of EAP proteins can help to restore the natural host immune defenses against S. aureus. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12528
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    ABSTRACT: The success of Staphylococcus aureus as a pathogen is partly attributable to its ability to thwart host innate immune responses, which includes resisting the antimicrobial functions of phagocytes. Here, we have studied the interaction of methicillin-resistant S. aureus (MRSA) strain USA300 with murine RAW 264.7 and primary human macrophages using molecular imaging and single cell analysis to obtain an unprecedented understanding of the interaction between the macrophage and MRSA. Herein we demonstrate that macrophages fail to control intracellular infection by MRSA USA300 despite trafficking the bacteria into mature phagolysosomes. Using fluorescence-based proliferation assays we also show that intracellular staphylococci proliferate and that replication commences while the bacteria are residing in mature phagolysosomes hours after initial phagocytosis. Finally, live-cell fluorescence video microscopy allowed for unprecedented visual insight into the escape of MRSA from macrophages, demonstrating that the macrophages die through a pathway characterized by membrane blebbing and activation of caspase-3 followed by acquisition of the vital dye propidium iodide. Moreover, cell death precedes the emergence of MRSA from infected macrophages and these events can be ablated by prolonged exposure of infected phagocytes to gentamicin. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12527
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    ABSTRACT: Outer membrane vesicles (OMV) are critical elements in many host-cell/microbe interactions. Previous studies of the symbiotic association between Euprymna scolopes and Vibrio fischeri had shown that, within 12 h of colonizing crypts deep within the squid's light organ, the symbionts trigger an irreversible program of tissue development in the host. Here, we report that OMV produced by V. fischeri are powerful contributors to this process. The first detectable host response to the OMV is an increased trafficking of macrophage-like cells called hemocytes into surface epithelial tissues. We showed that exposing the squid to other Vibrio species fails to induce this trafficking; however, addition of a high concentration of their OMV, which can diffuse into the crypts, does. We also provide evidence that tracheal cytotoxin (TCT) release by the symbionts, which can induce hemocyte trafficking, is not part of the OMV cargo, suggesting two distinct mechanisms to induce the same morphogenesis event. By manipulating the timing and localization of OMV signal delivery, we showed that hemocyte trafficking is fully induced only when V. fischeri, the sole species able to reach and grow in the crypts, succeeds in establishing a sustained colonization. Further, our data suggest that the host detection of OMV serves as a symbiotic checkpoint prior to inducing irreversible morphogenesis.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12525
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    ABSTRACT: Adhesion to cells is the initial step in the infectious cycle of basically all pathogenic bacteria and, to do so, microorganisms have evolved surface molecules that target different cellular receptors. Brucella is an intracellular pathogen that infects a wide range of mammals whose virulence is completely dependent on the capacity to replicate in phagocytes. Although much has been done to elucidate how Brucella multiplies in macrophages, we still do not understand how bacteria invade epithelial cells to perform a replicative cycle or what adhesion molecules are involved in the process. We report the identification in Brucella abortus of a novel adhesin that harbors a bacterial immunoglobulin-like domain and demonstrate that this protein is involved in the adhesion to polarized epithelial cells such as the Caco-2 and MDCK models targeting the bacteria to the cell-cell interaction membrane. While deletion of the gene significantly reduced adhesion, overexpression dramatically increased it. Addition of the recombinant protein to cells induced cytoskeleton rearrangements and showed that this adhesin targets proteins of the cell-cell interaction membrane in confluent cultures.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12526
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    ABSTRACT: Recently, we demonstrated that intratracheal transplantation of human umbilical cord blood derived mesenchymal stem cells (MSCs) attenuates Escherichia (E) coli induced acute lung injury (ALI) primarily by down-modulating inflammation and enhancing bacterial clearance in mice. This study was done to elucidate the mechanism underlying the antibacterial effects of MSCs. The growth of E. coli in vitro was significantly inhibited only by MSCs or their conditioned medium with bacterial preconditioning, but not by fibroblasts or their conditioned medium. Microarray analysis identified significant up-regulation of toll like receptors (TLR)-2 and TLR-4, and β-defensin 2 (BD2) in MSCs compared with fibroblasts after E. coli exposure. The increased BD2 level and the in vitro antibacterial effects of MSCs were abolished by specific antagonist or by siRNA-mediated knockdown of TLR-4, but not TLR-2, and restored by BD2 supplementation. The in vivo down-modulation of the inflammatory response and enhanced bacterial clearance, increased BD2 secretion and the resultant protection against E. coli induced pneumonia observed only with MSCs, but not fibroblasts, transplantation in mice, were abolished by knockdown of TLR-4 with siRNA transfection. Our data indicate that BD2 secreted by the MSCs via the TLR-4 signaling pathway is one of the critical paracrine factors mediating their microbicidal effects against E. coli, both in vitro and in vivo. Furthermore, TLR-4 from the transplanted MSCs plays a seminal role in attenuating in vivo E. coli induced pneumonia and the ensuing ALI through both its anti-inflammatory and anti-bacterial effects. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12522
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    ABSTRACT: The adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) plays a key role in virulence of Bordetella pertussis. CyaA penetrates myeloid cells expressing the complement receptor 3 (αM β2 integrin CD11b/CD18) and subverts bactericidal capacities of neutrophils and macrophages by catalyzing unregulated conversion of cytosolic ATP to the key signaling molecule cAMP. We show that the signaling of CyaA-produced cAMP hijacks, by an as yet unknown mechanism, the activity of the tyrosine phosphatase SHP-1 and activates the pro-apoptotic BimEL-Bax cascade. Mitochondrial hyperpolarization occurred in human THP-1 macrophages within 10 minutes of exposure to low CyaA concentrations (e.g. 20 ng ml(-1) ) and was accompanied by accumulation of BimEL and association of the pro-apoptotic factor Bax with mitochondria. BimEL accumulation required cAMP/PKA signaling, depended on SHP-1 activity and was selectively inhibited upon siRNA knockdown of SHP-1 but not of the SHP-2 phosphatase. Moreover, signaling of CyaA-produced cAMP inhibited the AKT/PKB pro-survival cascade, enhancing activity of the FoxO3a transcription factor and inducing Bim transcription. Synergy of FoxO3a activation with SHP-1 hijacking thus enables the toxin to rapidly trigger a persistent accumulation of BimEL, thereby activating the pro-apoptotic program of macrophages and subverting the innate immunity of the host. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12519
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    ABSTRACT: Export of most malaria proteins into the erythrocyte cytosol requires the Plasmodium Translocon of Exported proteins (PTEX) and a cleavable Plasmodium Export Element (PEXEL). In contrast, the contribution of PTEX in the liver stages and export of liver stage proteins is unknown. Here, using the FLP/FRT conditional mutatagenesis system, we generate transgenic P. berghei parasites deficient in EXP2, the putative pore-forming component of PTEX. Our data reveal that EXP2 is important for parasite growth in the liver and critical for parasite transition to the blood, with parasites impaired in their ability to generate a patent blood-stage infection. Surprisingly, whilst parasites expressing a functional PTEX machinery can efficiently export a PEXEL-bearing GFP reporter into the erythrocyte cytosol during a blood stage infection, this same reporter aggregates in large accumulations within the confines of the parasitophorous vacuole membrane during hepatocyte growth. Notably HSP101, the putative molecular motor of PTEX, could not be detected during the early liver stages of infection, which may explain why direct protein translocation of this soluble PEXEL-bearing reporter or indeed native PEXEL proteins into the hepatocyte cytosol has not been observed. This suggests that PTEX function may not be conserved between the blood and liver stages of malaria infection. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12520
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    ABSTRACT: Parasite effector proteins target various host cell compartments to alter host processes and promote infection. How effectors cross membrane-rich interfaces to reach these compartments is a major question in effector biology. Growing evidence suggests that effectors use molecular mimicry to subvert host cell machinery for protein sorting. We recently identified CTP1 (chloroplast-targeted protein 1), a candidate effector from the poplar leaf rust fungus Melampsora larici-populina that carries a predicted transit peptide and accumulates in chloroplasts and mitochondria. Here, we show that the CTP1 transit peptide is necessary and sufficient for accumulation in the stroma of chloroplasts. CTP1 is part of a Melampsora-specific family of polymorphic secreted proteins. Two members of that family, CTP2 and CTP3, also translocate in chloroplasts in a N-terminal signal-dependent manner. CTP1, CTP2 and CTP3 are cleaved when they accumulate in chloroplasts, while they remain intact when they do not translocate into chloroplasts. Our findings reveal that fungi have evolved effector proteins that mimic plant-specific sorting signals to traffic within plant cells. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12530
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    ABSTRACT: STAT3 imparts a profound influence on both the epithelial and immune components of the gastric mucosa, and through regulation of key intracellular signal transduction events, is well-placed to control inflammatory and oncogenic outcomes in the context of H. pylori infection. Here we review the roles of STAT3 in the host immune response to H. pylori infection, from both gastric mucosal and systemic perspectives, as well as alluding more specifically to STAT3-dependent mechanisms that might be exploited as drug targets. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 09/2015; DOI:10.1111/cmi.12518.
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    ABSTRACT: Anaplasma phagocytophilum is an emerging human pathogen and obligate intracellular bacterium. It inhabits a host cell-derived vacuole and cycles between replicative RC (reticulate cell) and infectious DC (dense-cored) morphotypes. Host-pathogen interactions that are critical for RC-to-DC conversion are undefined. We previously reported that A. phagocytophilum recruits GFP-tagged Rab10, a GTPase that directs exocytic traffic from the sphingolipid-rich trans-Golgi network (TGN), to its vacuole in a guanine nucleotide-independent manner. Here, we demonstrate that endogenous Rab10-positive TGN vesicles are not only routed to but also delivered into the A. phagocytophilum-occupied vacuole (ApV). Consistent with this finding, A. phagocytophilum incorporates sphingolipids while intracellular and retains them when naturally released from host cells. TGN vesicle delivery into the ApV is Rab10-dependent, upregulates expression of the DC-specific marker, APH1235, and is critical for the production of infectious progeny. The A. phagocytophilum surface protein, uridine monophosphate kinase, was identified as a guanine nucleotide-independent, Rab10-specific ligand. These data delineate why Rab10 is important for the A. phagocytophilum infection cycle and expands understanding of the benefits exploiting host cell membrane traffic affords intracellular bacterial pathogens. This article is protected by copyright. All rights reserved.
    Cellular Microbiology 08/2015; DOI:10.1111/cmi.12500