Interference with annexin II has no effect on entry of human cytomegalovirus into fibroblast cells.

Pietropaolo, Robin L.; Compton, Teresa

doi:10.1099/0022-1317-80-7-1807

Cited by 27 publications

(21 citation statements)

References 45 publications

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“…AnxA2 was reported to interact with HCMV glycoprotein B (Bold et al, 1996;Pietropaolo and Compton, 1997), and, together with S100A10, to facilitate CMV infection (Derry et al, 2007) probably through enhanced fusion of the virus with the host cell (Raynor et al, 1999). However, this was not confirmed in another study (Pietropaolo and Compton, 1999). AnxA2 on the host cell surface was also implicated in the entry of enterovirus type 71 (EV71), the causative agent of the hand, foot, and mouth disease, to the host cell surface, possibly by binding the viral capsid protein VP1 on the cell surface (Yang et al, 2011).…”

Section: Annexins As Host Cell Surface Receptors For Microbescontrasting

confidence: 47%

“…AnxA5 is associated with herpes simplex virus (HSV) type 1 (Loret et al, 2008), HIV-1 (Chertova et al, 2006), VSV (Moerdyk-Schauwecker et al, 2009, Rift Valley fever virus (Nuss et al, 2014), and IAV (Shaw et al, 2008). How and at which stage in the virus infection cycle annexins are acquired remains so far unclear (which Gershom et al, 2012Wright et al, 1994Wright et al, 1995;Pietropaolo and Compton 1997;Pietropaolo and Compton 1999;Raynor et al, 1999;Varnum et al, 2004;Derry et al, 2007 generally holds true for virus-embedded host cell proteins), and the association might simply reflect the nature of the specialized membrane domains where viral assembly and budding take place. Viruses that bud from lipidenriched plasma membrane domains ('rafts') would then incorporate the often raft-associated annexins as part of their host cell membrane-derived viral envelope.…”

Section: Annexins As Host Cell Derived Virulence Factorsmentioning

confidence: 99%

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Emerging functions as host cell factors – an encyclopedia of annexin-pathogen interactions

Kuehnl

Musiol

Raabe

et al. 2016

Biological Chemistry

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Abstract:Emerging infectious diseases and drug-resistant infectious agents call for the development of innovative antimicrobial strategies. With pathogenicity now considered to arise from the complex and bi-directional interplay between a microbe and the host, host cell factor targeting has emerged as a promising approach that might overcome the limitations of classical antimicrobial drug development and could open up novel and efficient therapeutic strategies. Interaction with and modulation of host cell membranes is a recurrent theme in the host-microbe relationship. In this review, we provide an overview of what is currently known about the role of the Ca 2+ dependent, membrane-binding annexin protein family in pathogenhost interactions, and discuss their emerging functions as host cell derived auxiliary proteins in microbe-host interactions and host cell targets.

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Section: Annexins As Host Cell Surface Receptors For Microbescontrasting

confidence: 47%

Section: Annexins As Host Cell Derived Virulence Factorsmentioning

confidence: 99%

Emerging functions as host cell factors – an encyclopedia of annexin-pathogen interactions

Kuehnl

Musiol

Raabe

et al. 2016

Biological Chemistry

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“…(iv) HCMV gB also forms a stable interaction with cellular annexin II (31). At present we favor a role of this interaction in virus maturation and egress (30). Clearly a collection of mutants will be extremely useful in creating a functional map for this essential and multifunctional protein.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Panel of Insertion Mutants in Human Cytomegalovirus Glycoprotein B

Singh

Compton

2000

J Virol

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Glycoprotein B (gB; gpUL55) of human cytomegalovirus (HCMV) plays a critical role in virus entry and cell-to-cell spread of infection. To define the structure-function relationships in gB, a panel of linker-insertion mutations was generated throughout the coding region. This strategy yielded a panel of 22 mutants with four amino acid insertions and 3 large truncation mutants. Assessment of the mutant proteins' biosynthetic properties and folding patterns analyzed in context with predicted secondary features revealed novel insights into gB's structure and trafficking properties. All of the insertion mutants were able to assemble into oligomers, suggesting that oligomerization is tolerant of small insertions and/or that multiple regions of the protein may be involved. Computer algorithm predictions of gB's secondary structure indicate that the furin-recognized cleavage site falls within an exposed loop. This loop may be particularly sensitive to structural alterations, since insertions upstream and downstream of the cleavage site rendered the mutant proteins cleavage defective. In addition, a strong correlation existed between terminal folding and cleavage of gB. Interestingly, terminal folding was not correlated with delivery to the cell surface but may influence the rate of transport to the cell surface. Nine mutants, containing insertions in both the extracellular and intracellular portions of gB, retained wild-type structural properties. This panel of characterized gB mutants, the first of this type for an HCMV protein, will be a useful tool in dissecting the role of gB during HCMV infection.Human cytomegalovirus (HCMV), a member of the Herpesviridae, is a ubiquitous pathogen that causes significant morbidity and mortality in immunocompromised individuals (1). The frequency and severity of HCMV diseases and the paucity of desirable therapeutic options indicate the need to identify and understand the structures and functions of key potential antiviral targets. An ideal target for either prevention or therapy would be to block entry and/or cell-to-cell spread of HCMV into and between cells. To rationally develop drugs, a detailed understanding of the viral and cellular components necessary for virus entry is needed. While HCMV entry is not completely understood, significant progress has been made in recent years identifying the major viral components involved in entry (reviewed in reference 13). Entry of HCMV into host cells requires a complex series of sequential interactions between multiple viral and cellular molecules (7,13,28). Viral entry can be divided into two distinct stages: attachment and penetration. Virus binding to heparan sulfate proteoglycans (HSPGs) is the initial step in the entry pathway (15,27). Virus bound to cell surface HSPG is rapidly converted to a more stable binding state likely mediated by interaction of the virion with a second cellular receptor (15). Once stably attached, the virion penetrates into the cell by direct fusion of the virus envelope and the cellular plasma membrane (14)...

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“…Annexin 2 has been associated with numerous virus species. In HCMV, it has been shown to be associated with gB (45), although its role during entry is still controversial (12,44). In the future, it will be important to validate the presence of these proteins and ultimately address their putative function for the virion.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Characterization of Bovine Herpesvirus 4 Extracellular Virions

Lété

Palmeira

Leroy

et al. 2012

J Virol

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cGammaherpesviruses are important pathogens in human and animal populations. During early events of infection, these viruses manipulate preexisting host cell signaling pathways to allow successful infection. The different proteins that compose viral particles are therefore likely to have critical functions not only in viral structures and in entry into target cell but also in evasion of the host's antiviral response. In this study, we analyzed the protein composition of bovine herpesvirus 4 (BoHV-4), a close relative of the human Kaposi's sarcoma-associated herpesvirus. Using mass spectrometry-based approaches, we identified 37 viral proteins associated with extracellular virions, among which 24 were resistant to proteinase K treatment of intact virions. Analysis of proteins associated with purified capsid-tegument preparations allowed us to define protein localization. In parallel, in order to identify some previously undefined open reading frames, we mapped peptides detected in whole virion lysates onto the six frames of the BoHV-4 genome to generate a proteogenomic map of BoHV-4 virions. Furthermore, we detected important glycosylation of three envelope proteins: gB, gH, and gp180. Finally, we identified 38 host proteins associated with BoHV-4 virions; 15 of these proteins were resistant to proteinase K treatment of intact virions. Many of these have important functions in different cellular pathways involved in virus infection. This study extends our knowledge of gammaherpesvirus virions composition and provides new insights for understanding the life cycle of these viruses.

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Interference with annexin II has no effect on entry of human cytomegalovirus into fibroblast cells.

Cited by 27 publications

References 45 publications

Emerging functions as host cell factors – an encyclopedia of annexin-pathogen interactions

Emerging functions as host cell factors – an encyclopedia of annexin-pathogen interactions

Characterization of a Panel of Insertion Mutants in Human Cytomegalovirus Glycoprotein B

Proteomic Characterization of Bovine Herpesvirus 4 Extracellular Virions

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