Sammanfattning

The gene encoding a plasma protein receptor from Streptococcus dysgalactine has been cloned and sequenced. The gene product, with a predicted molecular mass of approx. 44 kDa, binds alpha(2)-macroglobulin (alpha(2)M), serum albumin and immunoglobulin G (IgG). By subcloning and expressing various parts of the gene as fusion proteins, we found that the three binding activities reside in discrete domains of the protein. The single IgG-binding domain, localized in the C-terminal part of the molecule, shows high homology to streptococcal type-III Fc receptors. In the middle of the molecule, there is a stretch of 50 amino acids (aa) mediating albumin binding. This region has partial homology with the albumin-binding domains of streptococcal protein G. The alpha(2)M-binding domain is located in the N terminus of the molecule and is composed of a unique aa sequence. We call this trifunctional plasma protein receptor, MAG (binds alpha(2)M, albumin and IgG).

Nyckelord

REECOMBINANT DNA; BACTERIAL FC RECEPTOR; NUCLEOTIDE SEQUENCE; GENE FUSION; GENE STRUCTURE

Publicerad i

Gene
1994, Volym: 143, nummer: 1, sidor: 85-89
Utgivare: ELSEVIER SCIENCE BV

SLU författare

• Jonsson, Hans

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    

• Frykberg, Lars

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    

• Guss, Bengt

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Biokemi och molekylärbiologi
Mikrobiologi
Medicinsk biovetenskap


Publikationens identifierare

DOI: https://doi.org/10.1016/0378-1119(94)90609-2

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/79304