謎の抗体 ライム病と子宮頸がんワクチンに共通する何か

これは、ライム病の患者の臀部にできたマークです。

 

これも、ライム病の患者で、背中にできたマークです。

妊娠線とは違うということですが、見かけは妊娠線に似ています。

 

マダニに咬まれて、マダニやライム菌に対する抗体ができると、

この抗体が、コラーゲン周辺の何かに反応すると考えてよいのでしょうか。

（牛肉アレルギーはマダニに咬まれて、マダニの食道にある糖鎖に対する抗体ができていました。）

 

これに似た症状が、子宮頸がんワクチンの副反応でも複数報告されています。

ステロイド使用前です。

ステロイドの治療で、消えたと聞きました。（日本）

 

 

As we learned earlier, the body releases cytokines as a result of antigens the Lyme bacteria release - inflammation. What you may not have known is that the Lyme bacteria is so intelligent and evolved, it actually intentionally releases antigens so the immune system releases more cytokines, and for the bacteria, the release of more cytokines results in tissue (collagen) breakdown - the Lyme bacteria’s favorite food.

 

コラーゲンの糖鎖

 

 

Mol Cell Biol. 2009 Feb;29(4):943-52. doi: 10.1128/MCB.02085-07. Epub 2008 Dec 15.

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

Schegg B¹, Hülsmeier AJ, Rutschmann C, Maag C, Hennet T.

Author information

Abstract

Collagen is a trimer of three left-handed alpha chains representing repeats of the motif Gly-X-Y, where (hydroxy)proline and (hydroxy)lysine residues are often found at positions X and Y. Selected hydroxylysines are further modified by the addition of galactose and glucose-galactose units. Collagen glycosylation takes place in the endoplasmic reticulum before triple-helix formation and is mediated by beta(1-O)galactosyl- and alpha(1-2)glucosyltransferase enzymes. We have identified two collagen galactosyltransferases using affinity chromatography and tandem mass spectrometry protein sequencing. The two collagen beta(1-O)galactosyltransferases corresponded to the GLT25D1 and GLT25D2 proteins. Recombinant GLT25D1 and GLT25D2 enzymes showed a strong galactosyltransferase activity toward various types of collagen and toward the serum mannose-binding lectin MBL, which contains a collagen domain. Amino acid analysis of the products of GLT25D1 and GLT25D2 reactions confirmed the transfer of galactose to hydroxylysine residues. The GLT25D1 gene is constitutively expressed in human tissues, whereas the GLT25D2 gene is expressed only at low levels in the nervous system. The GLT25D1 and GLT25D2 enzymes are similar to CEECAM1, to which we could not attribute any collagen galactosyltransferase activity. The GLT25D1 and GLT25D2 genes now allow addressing of the biological significance of collagen glycosylation and the importance of this posttranslational modification in the etiology of connective tissue disorders.