Pinelady
Frequent Contributor (5K+ posts)
Member # 18524
posted
ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family. http://www.ncbi.nlm.nih.gov/pubmed/23722838 cta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):624-8. doi: 10.1107/S1744309113013249. Epub 2013 May 23.
Caesar JJ, Johnson S, Kraiczy P, Lea SM. Source
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, England. Abstract
Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America.
The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs),
to aid evasion of the human complement system
by recruiting and presenting complement regulator factor H
on its surface in a manner that mimics host cells.
Presented here is the atomic resolution structure of a member of this protein family, ErpC.
The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans.
It also describes the architecture of other CRASP proteins
belonging to the OspE/F-related paralogous protein family
and suggests that they have evolved to bind specific complement proteins,
aiding survival of the bacterium in different hosts. -------------
-------------------- Suspected Lyme 07 Test neg One band migrating in IgG region unable to identify.Igenex Jan.09IFA titer 1:40 IND IgM neg pos 31 +++ 34 IND 39 IND 41 IND 83-93 + DX:Neuroborreliosis Posts: 5850 | From Kentucky | Registered: Dec 2008
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Pinelady
Frequent Contributor (5K+ posts)
Member # 18524
posted
Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi.
Caesar JJ, Wallich R, Kraiczy P, Zipfel PF, Lea SM. Source
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, England. Abstract
Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems
across its range of reservoir hosts,
including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1).
Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known
and shows the formation of a homodimeric species
which is required for binding.
Mutagenesis studies have mapped a putative factor H binding site to a cleft
between the two subunits.
Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging
-------------------- Suspected Lyme 07 Test neg One band migrating in IgG region unable to identify.Igenex Jan.09IFA titer 1:40 IND IgM neg pos 31 +++ 34 IND 39 IND 41 IND 83-93 + DX:Neuroborreliosis Posts: 5850 | From Kentucky | Registered: Dec 2008
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