Re: Interplay between Virus and Candida

[Guest guest]

there was a long article in one of the journals recently on

'competition' for cell membrane receptors between various viral proteins

and bacterial lps .... and it also stressed interactions between various

cell receptors, and how opening one (by getting rid of a viral protein

that binds to it) can upregulate another receptor, making cell more

vulnerable to bacterial toxins... The general conclusion was similar to

this abstract, but different mechanism involved (hypothesised, as all

observations were in vitro).

There was no mention of fungal involvement, but I see no reason why

there would not be one.

Natasa

> > >

> > > just came across these very interesting abstracts... (sadly not

much

> > > follow-up research on the subject in other viruses to be found).

> > >

> > > the last abstract in particular could go towards explaining why

> > > increased yeast symptoms when lowering viral load...

> > >

> > > (no idea how this could affect treatments but still thought it was

> > > interesting)

> > >

> > > Natasa

> > >

> > > J Infect Dis. 1997 Aug;176(2):492-8.

> > >

> > > WŸrzner R, Gruber A, Stoiber H, Spruth M, Chen YH,

Lukasser-Vogl E,

> > > Schwendinger MG, Dierich MP. Institut fŸr Hygiene, University

of

> > > Innsbruck, Austria.

> > >

> > > Oral candidiasis in human immunodeficiency virus type 1

> > > (HIV-1)-infected persons is believed to be caused by the acquired

T

> > > lymphocyte immunodeficiency. The direct interaction of C. albicans

and

> > > HIV-1 in vitro was investigated. Twice as many yeasts adhered to

cells

> > > transfected with the HIV-1 env gene as they did to controls. HIV-1

> > > rsgp160 and rsgp41 but not rsgp120 were found to bind to Candida

> > > albicans via two C3-like regions within gp41. Normal human serum,

but

> > > not C3-depleted serum, was able to inhibit rsgp41 binding to C.

> > > albicans. Vice versa, rsgp160 and rsgp41 were able to block

rosetting of

> > > C. albicans with iC3b-coated sheep erythrocytes. Binding to C.

albicans,

> > > and its inhibition by rsgp41 or rsgp160, was confirmed for the

whole

> > > virus. Therefore, oral candidiasis in HIV-1-infected subjects may

be

> > > augmented or may even be initiated by direct interaction between

C.

> > > albicans and HIV-1 or HIV-1-infected cells.

> > >

> > > PMID: 9237717 [PubMed - indexed for MEDLINE]

> > >

> > >

> > > J Infect Dis. 1998 Apr;177(4):1057-63.Links

> > >

> > > Human immunodeficiency virus type 1 gp160 and gp41 binding to

> > > Candida albicans selectively enhances candidal virulence in vitro.

> > >

> > > Gruber A, Lukasser-Vogl E, Borg-von Zepelin M, Dierich MP,

> > > WŸrzner R. Institut fŸr Hygiene, University of Innsbruck,

> > > Austria.

> > >

> > > Previously, it has been shown that human immunodeficiency

virus

> > > (HIV)-1 envelope proteins gp160 and gp41 bind to Candida albicans.

> > > Whether this interaction affects candidal virulence in vitro was

> > > investigated. HIV-1 gp160 or gp120 treatment of C. albicans

> > > significantly altered neither growth nor phospholipase activity of

the

> > > fungus. However, treatment of C. albicans with gp160, but not with

> > > gp120, led to an elevation of free and cell-bound aspartate

proteinase.

> > > In addition, culture supernatants obtained from C. albicans

treated with

> > > gp160 or gp41, but not with gp120, showed a strong increase in

> > > proteinase activity. Finally, C. albicans viable yeast cells

treated

> > > with gp160 or gp41 and serum were phagocytosed by

polymorphonuclear

> > > leukocytes to a lesser extent than was C. albicans treated with

gp120

> > > and serum or serum alone. These findings suggest that the

interaction

> > > between HIV-1 gp160 and C. albicans may promote the virulence of

C.

> > > albicans in HIV-1-positive patients.

> > >

> > > PMID: 9534982 [PubMed - indexed for MEDLINE]

> > >

> > >

> > > FEMS Immunol Med Microbiol. 2003 Jun 10;37(1):77-83.

> > >

> > > HIV-1 and its transmembrane protein gp41 bind to different

Candida

> > > species modulating adhesion.

> > >

> > > Gruber A, Lell CP, Spruth M, Lass-Flšrl C, Speth C,

Stoiber H,

> > > Hube B, D, Polonelli L, Dierich MP, WŸrzner R.

Institute

> > > for Hygiene and Social Medicine, University of Innsbruck, and

Ludwig

> > > Boltzmann Institute for AIDS Research, Innsbruck, Austria.

> > >

> > > Oral candidiasis in HIV-1-infected individuals is widely

believed to

> > > be triggered by the acquired T-lymphocyte immunodeficiency.

Recently,

> > > binding of the HIV-1 envelope protein gp160 and its subunit gp41,

and

> > > also of the whole virus itself, to Candida albicans has been

shown. The

> > > present study shows that, in addition to C. albicans, HIV-1 gp41

also

> > > binds to yeast and hyphal forms of Candida dubliniensis, a species

which

> > > is closely related to C. albicans, and to Candida tropicalis but

not to

> > > Candida krusei, Candida glabrata or Saccharomyces cerevisiae. The

> > > previous finding that gp41 binding to C. albicans augments fungal

> > > virulence in vitro is supported by the observation that the yeast

showed

> > > an enhanced adhesion to HIV-infected H9 cells in comparison to

> > > uninfected cells. In line with these results soluble gp41 itself

reduced

> > > binding of C. albicans to both endothelial and epithelial cell

lines,

> > > confirming a dominant role of the gp41 binding moiety on the

surface of

> > > Candida for adhesion. Surface-associated secreted aspartic

proteinases

> > > (Saps) play an important role in candidial adhesion, but are not

likely

> > > to be involved in the interaction as gp41 binding to the C.

albicans

> > > parental wild-type strain was comparable to that of three

different

> > > isogenic Sap deletion mutants. Furthermore, gp41 binding to the

yeast

> > > killer toxin-susceptible C. albicans strain 10S was not

inhibitable by

> > > an anti-YKT receptor antibody. In conclusion, HIV-1 interacts with

> > > different clinically important Candida spp., and may thereby

affect the

> > > outcome of the respective fungal infection.

> > >

> > > PMID: 12770763 [PubMed - indexed for MEDLINE]

> > >

> > > .... The results of this study suggest that HIV infection is

associated

> > > with the selection of strains of C. albicans with and increased

ability

> > > to adhere to oral mucosa.

> > > PMID: 7473680 [PubMed - indexed for MEDLINE]

> > >

> >

>

[Guest guest]

We might expect it to all work out most of the time when we have good nutrition and are living away from pollution.there was a long article in one of the journals recently on'competition' for cell membrane receptors between various viral proteinsand bacterial lps .... and it also stressed interactions between variouscell receptors, and how opening one (by getting rid of a viral proteinthat binds to it) can upregulate another receptor, making cell morevulnerable to bacterial toxins... The general conclusion was similar tothis abstract, but different mechanism involved (hypothesised, as allobservations were in vitro).There was no mention of fungal involvement, but I see no reason whythere would not be one.Natasa>> One back at you.>> Nature. 2007 May 17;447(7142):326-9. Links> Herpesvirus latency confers symbiotic protection from bacterialinfection.

[Guest guest]

Please help me to understand this (way over my head at the moment). If the dormant herpes virus sets up a kind of shield against bacterial growth, does that mean that we should expect bacterial infections when addressing viral loads? Fungal overgrowth too? Or does that mean that the virus can impart protection from bacteria, only when the body has, "overcome" it? I'm confused, but I need to understand. Not only does our dgs have herpes, but I have noticed that everyone in our family develops horrible yeast overgrowth as they begin to get well from the flu. It looks like a relapse of the flu, but one with all the symptoms of yeast. Stan Kurtz wrote: One back at you.Nature. 2007 May 17;447(7142):326-9. LinksHerpesvirus latency confers symbiotic protection from bacterial infection.Barton ES, White DW, Cathelyn JS, Brett-McClellan KA, Engle M, Diamond MS, VL, Virgin HW 4th.Departments of Pathology and Immunology, Washington University Medical School, 660 South Euclid Avenue, St. Louis, Missouri 63110, USA.All humans become infected with multiple herpesviruses during childhood. After clearance of acute infection, herpesviruses enter a dormant state known as latency. Latency persists for the life of the host and is presumed to be parasitic, as it leaves the individual at risk for subsequent viral reactivation and disease. Here we show that herpesvirus latency also confers a surprising benefit to the host. Mice latently infected with either

murine gammaherpesvirus 68 or murine cytomegalovirus, which are genetically highly similar to the human pathogens Epstein-Barr virus and human cytomegalovirus, respectively, are resistant to infection with the bacterial pathogens Listeria monocytogenes and Yersinia pestis. Latency-induced protection is not antigen specific but involves prolonged production of the antiviral cytokine interferon-gamma and systemic activation of macrophages. Latency thereby upregulates the basal activation state of innate immunity against subsequent infections. We speculate that herpesvirus latency may also sculpt the immune response to self and environmental antigens through establishment of a polarized cytokine environment. Thus, whereas the immune evasion capabilities and lifelong persistence of herpesviruses are commonly viewed as solely pathogenic, our data suggest that latency is a symbiotic relationship with immune benefits for the

host.PMID: 17507983 [PubMed - indexed for MEDLINE]> >> > just came across these very interesting abstracts... (sadly not much> > follow-up research on the subject in other viruses to be found).> > > > the last abstract in particular could go towards explaining why> > increased yeast symptoms when lowering viral load...> > > > (no idea how this could affect treatments but still thought it was> > interesting)> > > > Natasa> > > > J Infect Dis. 1997 Aug;176(2):492-8.> > > > WŸrzner R, Gruber

A, Stoiber H, Spruth M, Chen YH, Lukasser-Vogl E,> > Schwendinger MG, Dierich MP. Institut fŸr Hygiene, University of> > Innsbruck, Austria.> > > > Oral candidiasis in human immunodeficiency virus type 1> > (HIV-1)-infected persons is believed to be caused by the acquired T> > lymphocyte immunodeficiency. The direct interaction of C. albicans and> > HIV-1 in vitro was investigated. Twice as many yeasts adhered to cells> > transfected with the HIV-1 env gene as they did to controls. HIV-1> > rsgp160 and rsgp41 but not rsgp120 were found to bind to Candida> > albicans via two C3-like regions within gp41. Normal human serum, but> > not C3-depleted serum, was able to inhibit rsgp41 binding to C.> > albicans. Vice versa, rsgp160 and rsgp41 were able to block rosetting of> > C. albicans with iC3b-coated sheep erythrocytes. Binding to C.

albicans,> > and its inhibition by rsgp41 or rsgp160, was confirmed for the whole> > virus. Therefore, oral candidiasis in HIV-1-infected subjects may be> > augmented or may even be initiated by direct interaction between C.> > albicans and HIV-1 or HIV-1-infected cells.> > > > PMID: 9237717 [PubMed - indexed for MEDLINE]> > > > > > J Infect Dis. 1998 Apr;177(4):1057-63.Links> > > > Human immunodeficiency virus type 1 gp160 and gp41 binding to> > Candida albicans selectively enhances candidal virulence in vitro.> > > > Gruber A, Lukasser-Vogl E, Borg-von Zepelin M, Dierich MP,> > WŸrzner R. Institut fŸr Hygiene, University of Innsbruck,> > Austria.> > > > Previously, it has been shown that human immunodeficiency virus> > (HIV)-1 envelope proteins gp160 and gp41 bind to Candida

albicans.> > Whether this interaction affects candidal virulence in vitro was> > investigated. HIV-1 gp160 or gp120 treatment of C. albicans> > significantly altered neither growth nor phospholipase activity of the> > fungus. However, treatment of C. albicans with gp160, but not with> > gp120, led to an elevation of free and cell-bound aspartate proteinase.> > In addition, culture supernatants obtained from C. albicans treated with> > gp160 or gp41, but not with gp120, showed a strong increase in> > proteinase activity. Finally, C. albicans viable yeast cells treated> > with gp160 or gp41 and serum were phagocytosed by polymorphonuclear> > leukocytes to a lesser extent than was C. albicans treated with gp120> > and serum or serum alone. These findings suggest that the interaction> > between HIV-1 gp160 and C. albicans may promote the virulence of

C.> > albicans in HIV-1-positive patients.> > > > PMID: 9534982 [PubMed - indexed for MEDLINE]> > > > > > FEMS Immunol Med Microbiol. 2003 Jun 10;37(1):77-83.> > > > HIV-1 and its transmembrane protein gp41 bind to different Candida> > species modulating adhesion.> > > > Gruber A, Lell CP, Spruth M, Lass-Flšrl C, Speth C, Stoiber H,> > Hube B, D, Polonelli L, Dierich MP, WŸrzner R. Institute> > for Hygiene and Social Medicine, University of Innsbruck, and Ludwig> > Boltzmann Institute for AIDS Research, Innsbruck, Austria.> > > > Oral candidiasis in HIV-1-infected individuals is widely believed to> > be triggered by the acquired T-lymphocyte immunodeficiency. Recently,> > binding of the HIV-1 envelope protein gp160 and its subunit gp41, and> > also of the whole virus

itself, to Candida albicans has been shown. The> > present study shows that, in addition to C. albicans, HIV-1 gp41 also> > binds to yeast and hyphal forms of Candida dubliniensis, a species which> > is closely related to C. albicans, and to Candida tropicalis but not to> > Candida krusei, Candida glabrata or Saccharomyces cerevisiae. The> > previous finding that gp41 binding to C. albicans augments fungal> > virulence in vitro is supported by the observation that the yeast showed> > an enhanced adhesion to HIV-infected H9 cells in comparison to> > uninfected cells. In line with these results soluble gp41 itself reduced> > binding of C. albicans to both endothelial and epithelial cell lines,> > confirming a dominant role of the gp41 binding moiety on the surface of> > Candida for adhesion. Surface-associated secreted aspartic proteinases> > (Saps) play an

important role in candidial adhesion, but are not likely> > to be involved in the interaction as gp41 binding to the C. albicans> > parental wild-type strain was comparable to that of three different> > isogenic Sap deletion mutants. Furthermore, gp41 binding to the yeast> > killer toxin-susceptible C. albicans strain 10S was not inhibitable by> > an anti-YKT receptor antibody. In conclusion, HIV-1 interacts with> > different clinically important Candida spp., and may thereby affect the> > outcome of the respective fungal infection.> > > > PMID: 12770763 [PubMed - indexed for MEDLINE]> > > > .... The results of this study suggest that HIV infection is associated> > with the selection of strains of C. albicans with and increased ability> > to adhere to oral mucosa.> > PMID: 7473680 [PubMed - indexed for MEDLINE]>

>>

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