to cleavde immune complexes, circulating and those embedded in tissue, see, mucos.de, and selct british icon or language of choice...studies on plant and animal enzymes to cleave and clear i.c. if i recall correctly, papain and bromelain may get embeded ICs.
wobenzym, and other enzymatic preps. evaluated here. best to read essays on which formulation to use, as anything with trypsin and chymotrypsin in it will keep inflammation at a low leve; with high-, and/ and or embedded ic having trypsin and chymotrypsi in enzymatic prep. may not be desirable,depending on phase of a given illness. sse company eval. for use of preps. accross medial conditions.
one contraindicaton i recal:
use of these close in time to surgery, including dental extactions, as these preps will cause extended bleeding time; there are other contraindications with some meds. check lit. on this, and company for miore on this.
-------------------- pingpong Posts: 361 | From At the Pingpong Tournament | Registered: Oct 2007
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I was the one who posted that other thread you mentioned.
In the end what I found with my research is there is no clear cut answer. Dr J definitely feels strongly about Band 18, but it's one of many indicators of Lyme.
You'll need to combine your blood test results with your SYMPTOMS to come up with a diagnosis.
In my case I felt fortunate to have Band 18+ because I believe Dr J's research and that it is a clear indicator of Lyme. Therefore I pushed my GP to treat me. I'm at about 5 months of abx now and doing really well. Most things have cleared up.
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That (Lyme) band is associated with a complement binding protein.. see the references below
Whether or not it's cross reactive with anything else- I don't know.
Read on.... Barb
REFERENCE 1 Infect Immun. 2001 Dec;69(12):7800-9. Further characterization of complement regulator-acquiring surface proteins of Borrelia burgdorferi.Kraiczy P, Skerka C, Brade V, Zipfel PF. Institute of Medical Microbiology, University Hospital of Frankfurt, D-60596 Frankfurt, Germany. [email protected]
The three genospecies Borrelia burgdorferi, Borrelia garinii, and Borrelia afzelii, all causative agents of Lyme disease, differ in their susceptibilities to human complement-mediated lysis. We recently reported that serum resistance of borrelias correlates largely with their ability to bind the human complement regulators FHL-1/reconectin and factor H. To date, two complement regulator-acquiring-proteins (CRASP-1 and CRASP-2) have been identified in serum-resistant B. afzelii isolates (P. Kraiczy, C. Skerka, M. Kirschfink, V. Brade, and P. F. Zipfel, Eur. J. Immunol. 31:1674-1684, 2001). Here, we present a comprehensive study of the CRASPs detectable in both serum-resistant and intermediate serum-sensitive B. afzelii and B. burgdorferi isolates. These CRASPs were designated according to the genospecies either as BaCRASPs, when derived from B. afzelii, or as BbCRASPs, for proteins identified in B. burgdorferi isolates. Each borrelial isolate expresses distinct CRASPs that can be differentiated by their mobility and binding phenotypes. A detailed comparison reveals overlapping and even identical binding profiles for BaCRASP-1 (27.5 kDa), BbCRASP-1 (25.9 kDa), and BbCRASP-2 (23.2 kDa), which bind FHL-1/reconectin strongly and interact weakly with factor H. In contrast, two B. afzelii proteins (BaCRASP-4 [19.2 kDa] and BaCRASP-5 [22.5 kDa]) and three B. burgdorferi proteins (BbCRASP-3 [19.8 kDa], BbCRASP-4 [18.5 kDa], and BbCRASP-5 [17.7 kDa]) bind factor H but not FHL-1/reconectin. Most CRASPs bind both human immune regulators at their C-terminal ends. Temperature-dependent up-regulation of CRASPs (BaCRASP-1, BaCRASP-2, and BaCRASP-5) is detected in low-passage borrelias cultured at 33 or 37 degrees C compared with those cultured at 20 degrees C. The characterization of the individual CRASPs on the molecular level is expected to identify new virulence factors and potential vaccine candidates.
PMID: 11705962 [PubMed - indexed for MEDLINE]
REFERENCE 2 Mol Microbiol. 2006 Sep;61(5):1220-36
Functional characterization of BbCRASP-2, a distinct outer membrane protein of Borrelia burgdorferi that binds host complement regulators factor H and FHL-1.Hartmann K, Corvey C, Skerka C, Kirschfink M, Karas M, Brade V, Miller JC, Stevenson B, Wallich R, Zipfel PF, Kraiczy P. Institute of Medical Microbiology, University Hospital of Frankfurt, Paul-Ehrlich-Str. 40, 60596 Frankfurt, Germany.
Borrelia burgdorferi, the aetiological agent of Lyme disease, employs sophisticated means to survive in diverse mammalian hosts. Recent studies demonstrated that acquisition of complement regulators factor H and factor H-like protein-1 (FHL-1) allows spirochetes to resist complement-mediated killing. Serum-resistant B. burgdorferi express up to five distinct complement regulator-acquiring surface proteins (CRASPs) that bind factor H and/or FHL-1. In this study we have identified and characterized one of those B. burgdorferi proteins, named BbCRASP-2. BbCRASP-2 is distinct from the four previously identified factor H/FHL-1-binding CRASPs of B. burgdorferi strains. The single copy of the gene encoding BbCRASP-2, cspZ, is located on the linear plasmid lp28-3. BbCRASP-2 is highly divergent from the factor H/FHL-1-binding protein BbCRASP-1 and from members of the factor H-binding Erp (OspE/F-related) protein family. Peptide mapping analysis revealed that the factor H/FHL-1 binding site is discontinuous and it was found that C-terminal truncations abrogate factor H and FHL-1 binding. The predominant BbCRASP-2 binding site of both host complement regulators was mapped to the short consensus repeat 7 (SCR 7). Factor H and FHL-1 bound to BbCRASP-2 maintain cofactor activity for factor I-mediated C3b inactivation and accelerate the decay of the C3 convertase. Expression of BbCRASP-2 in serum-sensitive B. burgdorferi mutant B313 increased resistance to complement-mediated lysis. The characterization of BbCRASP-2 now provides a complete picture of the three diverse complement regulator-binding protein families of B. burgdorferi yielding new insights into the pathogenesis of Lyme disease.
PMID: 16925556 [PubMed - indexed for MEDLINE]
Related LinksComplement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins. [J Biol Chem. 2004]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. [Eur J Immunol. 2003]Further characterization of complement regulator-acquiring surface proteins of Borrelia burgdorferi. [Infect Immun. 2001]Binding of human complement regulators FHL-1 and factor H to CRASP-1 orthologs of Borrelia burgdorferi. [Wien Klin Wochenschr. 2006]Immunological characterization of the complement regulator factor H-binding CRASP and Erp proteins of Borrelia burgdorferi. [Int J Med Microbiol. 2004]See all Related Articles...
Posts: 1873 | From VT | Registered: Oct 2002
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this is re: my son. he has allot of other circumstances and recent life events causing symptoms that could be related to depression and anxiety apart from lyme (some very serious circumstances).
however, there is then also a possibility of relapse under this stress. on the watch for that.
in the meantime, we're looking at the IgM band 18 he had show up, plus the inflammatory response, to also check the possibility of re-infection this past summer.
it's going to be pretty hard to figure out unless further diagnostic tools reveal more, or if symptoms start to differentiate themselves from those that overlap with everything else going on.
i happened upon doc sh. in fla's info, agreeing with jones that band 18 was considered rather difinitive for presence of bb. i suppose we'll consider reinfection a possibility and talk to the doctor.