Re: Immune evasion of Borrelia burgdorferi

[Guest guest]

hi Nelly,

I've been discussing possible direct antimicrobial effects of heparin

with a couple people recently, and PMIDs 12603746 and 14693545 came

up. It sounds as tho the safe use of heparin might require physician

monitoring - I know very little about it.

<janel@p...> wrote:

> I know immune evasion of Bb has often been mentioned. I also

know heparin has been used by some people as per Berg (Hemex) to

counteract the hypercoag situation people with chronic I & I find

themselves in.

>

> Has heparin treatment been discussed in this context?

>

> Nelly

>

>

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve & db=pubmed & dopt=Abstra\

ct & list_uids=12616490 & query_hl=1

>

>

> Eur J Immunol. 2003 Mar;33(3):697-707. Related Articles, Links

>

>

> Immune evasion of Borrelia burgdorferi: mapping of a

complement-inhibitor factor H-binding site of BbCRASP-3, a novel

member of the Erp protein family.

>

> Kraiczy P, Hellwage J, Skerka C, Kirschfink M, Brade V, Zipfel PF,

Wallich R.

>

> Institute of Medical Microbiology, University Hospital of furt,

-Ehrlich-Strasse 40, D-60596 furt, Germany. Kraiczy@e...

>

> The causative agents of Lyme disease, Borrelia burgdorferi s.s., B.

garinii, and B. afzelii, differ in their susceptibility to

complement-mediated lysis. This phenomenon apparently depends on the

expression of proteins termed complement regulator-acquiring surface

proteins (CRASP) and their binding to the inhibitory plasma proteins

factor H and FHL-1. To characterize these bacterial proteins in more

detail we have now isolated from a B. burgdorferi expression library a

novel factor H-binding protein. In accordance with our previous

studies this protein was termed BbCRASP-3 and represents a novel

member of the polymorphic Erp (OspE/F-related) protein family. On the

basis of protease accessibility assays using intact spirochetes,

BbCRASP-3 is identified as a surface-exposed protein and binds the

C-terminal short consensus repeats of factor H. Applying deletion

mutants of BbCRASP-3, the factor H-binding site was mapped to the

nine-amino-acid motif LEVLKKNLK localized at the C-terminal end of

BbCRASP-3. ******Factor H bound to BbCRASP-3 maintains its cofactor

activity in factor I-mediated C3b inactivation. *******Binding of

BbCRASP-3 to factor H can be inhibited by heparin, a physiological

ligand of the complement regulator factor H.******* Blocking of

factor-H-binding by soluble BbCRASP-3 leads to an increase of

complement deposition on intermediate serum-resistant strain ZS7. In

conclusion, BbCRASP-3 has been identified as a novel factor H-binding

protein on B. burgdorferi which by conferring complement resistance to

the pathogen may contribute to its persistence in the mammalian host.

>

> PMID: 12616490 [PubMed - indexed for MEDLINE]

[Guest guest]

Dumb question, is the factor H they talk about, heparin? I read some

stuff about heparin binding to Lyme and inhibiting it. I also just

found a recent study out of Japan on heparin totally clearing

Babesia. It's on my website in the Lyme section, along with tons of

stuff about heparin and hypercoagulation. There is a whole topci

forum on hypercoagualtion. The address is in the links section to

the left, thanks to Penny.

> > I know immune evasion of Bb has often been mentioned. I

also

> know heparin has been used by some people as per Berg

(Hemex) to

> counteract the hypercoag situation people with chronic I & I find

> themselves in.

> >

> > Has heparin treatment been discussed in this context?

> >

> > Nelly

> >

> >

> http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?

cmd=Retrieve & db=pubmed & dopt=Abstract & list_uids=12616490 & query_hl=1

> >

> >

> > Eur J Immunol. 2003 Mar;33(3):697-707. Related Articles,

Links

> >

> >

> > Immune evasion of Borrelia burgdorferi: mapping of a

> complement-inhibitor factor H-binding site of BbCRASP-3, a novel

> member of the Erp protein family.

> >

> > Kraiczy P, Hellwage J, Skerka C, Kirschfink M, Brade V, Zipfel

PF,

> Wallich R.

> >

> > Institute of Medical Microbiology, University Hospital of

furt,

> -Ehrlich-Strasse 40, D-60596 furt, Germany. Kraiczy@e...

> >

> > The causative agents of Lyme disease, Borrelia burgdorferi s.s.,

B.

> garinii, and B. afzelii, differ in their susceptibility to

> complement-mediated lysis. This phenomenon apparently depends on

the

> expression of proteins termed complement regulator-acquiring

surface

> proteins (CRASP) and their binding to the inhibitory plasma

proteins

> factor H and FHL-1. To characterize these bacterial proteins in

more

> detail we have now isolated from a B. burgdorferi expression

library a

> novel factor H-binding protein. In accordance with our previous

> studies this protein was termed BbCRASP-3 and represents a novel

> member of the polymorphic Erp (OspE/F-related) protein family. On

the

> basis of protease accessibility assays using intact spirochetes,

> BbCRASP-3 is identified as a surface-exposed protein and binds the

> C-terminal short consensus repeats of factor H. Applying deletion

> mutants of BbCRASP-3, the factor H-binding site was mapped to the

> nine-amino-acid motif LEVLKKNLK localized at the C-terminal end of

> BbCRASP-3. ******Factor H bound to BbCRASP-3 maintains its cofactor

> activity in factor I-mediated C3b inactivation. *******Binding of

> BbCRASP-3 to factor H can be inhibited by heparin, a physiological

> ligand of the complement regulator factor H.******* Blocking of

> factor-H-binding by soluble BbCRASP-3 leads to an increase of

> complement deposition on intermediate serum-resistant strain ZS7.

In

> conclusion, BbCRASP-3 has been identified as a novel factor H-

binding

> protein on B. burgdorferi which by conferring complement

resistance to

> the pathogen may contribute to its persistence in the mammalian

host.

> >

> > PMID: 12616490 [PubMed - indexed for MEDLINE]