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Haemophilus somnus undergoes antigenic and structural phase variation in its lipooligosaccharide (LOS). A gene (lob-1) containing repetitive 5'-CAAT-3' sequences that may, in part, contribute to phase variation was cloned and sequenced (T. J. Inzana et al., Infect. Immun. 65:4675-4681, 1997). We have now identified another putative gene (lob-2A) immediately(More)
The opacity factor positive M type 2 group A streptococcal isolate, A207, expresses a unique functional type II'o IgG-binding protein which reacts with all four human IgG subclasses and rabbit IgG. In order to determine the gene product or products responsible for this activity, three genes of the vir regulon from this isolate were cloned, expressed and(More)
  • T D Pack
  • Current protocols in immunology
  • 2001
This unit describes the purification of human immunoglobulin A (IgA).The main method utilizes an IgA-binding protein (IgA-bp) as an affinity reagent, similar to the IgG-binding proteins, protein A and protein G. An alternate protocol describes a method for isolating IgA1 using affinity column chromatography with Jacalin, an IgA1-specific lectin. Another(More)
The gene encoding the Enn protein (enn) of the M untypeable group A streptococcal (GAS) strain 64/14 was amplified by polymerase chain reaction, cloned into the expression vector pJLA602 and expressed in Escherichia coli DH5 alpha. Unlike other GAS-Enn proteins, which exhibit IgA-binding activity, the recombinant Enn enn64/14 protein reacted preferentially(More)
Sequence comparison of six known group-A streptococcal IgG-binding proteins, sharing the common property of protein G-inhibitable IgG3-binding-activity, identified a highly conserved 35-amino-acid (aa) sequence (74-100% similarity) within an EQ-rich central conserved core region of each protein. A search of aa sequence databases identified four additional(More)
Analysis of group A streptococcal immunoglobulin G (IgG)-binding protein reactivity with different human IgG3-myeloma proteins provided evidence for at least two functional forms of these molecules. Representative IgG3-binding molecules were isolated, biotinylated, and used as tracers in competitive binding assays. Cross-inhibition studies demonstrated the(More)
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