Re: for brent: genetic exchange in bb

and this:

..................................................................................................................

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 Frankfurt,
Paul-Ehrlich-Strasse 40, D-60596 Frankfurt, Germany.
Kraiczy@xxxxxxxxxxxxxxxxxxx

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]

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I guess you could say Bb s.s. is "DEF". It's da bomb!

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