1887

Abstract

SUMMARY

A phage-associated lysin (PAL) was used to release M protein from group-A streptococci of types 1 and 23. Much of the lysin-released-M protein (LYSIN-M) of both types was of high molecular weight, since LYSIN-M appeared just after the void volume on Sephadex G-200 gel-filtration. Some of the LYSIN-M of both types was found to be firmly attached to group-A carbohydrate. Type-1 LYSIN-M was partially purified by ammonium-sulphate precipitation followed by absorption and elution from an immunoabsorbent column containing antibody for group-A carbohydrate. Type-23 LYSIN-M was partially purified by precipitation at its isoelectric point, 4-9. Rabbits immunised in the footpads with either type-1 or type-23 LYSIN-M responded by producing both precipitins and bactericidal (opsonising) antibodies. Some of the antisera were absorbed and rendered specific for homologous acid extracts. The LYSIN-M preparations of both types 1 and 23 were originally contaminated with heat-labile antigen(s). Antibodies to these heat-labile antigen(s), which cross-react from type to type, were found in the type-specific antisera distributed by the Center for Disease Control. The specificity of Lancefield typing antisera depends on their being tested with extracts of streptococci prepared at and 100°C for 10 min. Although LYSIN-M is more difficult to prepare and purify than acid-heat released M protein, it might prove useful for studying the nature of native streptococcal M protein.

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/content/journal/jmm/10.1099/00222615-10-2-179
1977-05-01
2019-10-14
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http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-10-2-179
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