Abstract:
:Among the pathological effects in man following infection with Mycoplasma pneumoniae is a transient autoimmune disorder characterized by the presence of high-titre erythrocyte autoantibodies (cold agglutinins). These autoantibodies are usually directed against the carbohydrate antigen termed I (ref. 3) which consists of a branched oligosaccharide. The mechanism by which the anti-I antibodies are elicited is unknown. However, sialic acid-containing receptors have been implicated in the adherence of M. pneumoniae to erythrocytes and other cell types, and both I and the related antigen i occur on erythrocytes in sialylated form: i is the predominant antigen on fetal erythrocytes and I is predominant in adults. Anti-I antibodies might arise in M. pneumoniae infection in response to a modification of the 'self' antigen-I as a result of its interaction with this agent. Here we report our study of the specificity of the interaction of M. pneumoniae with human erythrocytes. We found that this interaction is mediated by long chain oligosaccharides of sialic acid joined by alpha 2-3 linkage to the terminal galactose residues of poly-N-acetyllactosamine sequences of Ii antigen type.
journal_name
Naturejournal_title
Natureauthors
Loomes LM,Uemura K,Childs RA,Paulson JC,Rogers GN,Scudder PR,Michalski JC,Hounsell EF,Taylor-Robinson D,Feizi Tdoi
10.1038/307560a0subject
Has Abstractpub_date
1984-02-09 00:00:00pages
560-3issue
5951eissn
0028-0836issn
1476-4687journal_volume
307pub_type
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