The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions.
To obtain iron from the host for growth, staphylococci have evolved sophisticated iron-scavenging systems including siderophores and a cell surface receptor for transferrin, the mammalian iron-transporting glycoprotein. The staphylococcal transferrin receptor has been identified as a member of a newly emerging family of multifunctional, cell-surface-associated glyceraldehyde-3-phosphate dehydrogenases, which not only retain their glycolytic enzyme activities but also bind diverse human serum proteins and possess NAD-ribosylating activity. These multiple functions suggest a potential contribution to virulence far beyond iron acquisition.
Modun
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Institute of Infections and Immunity, Queen's Medical Centre, University of Nottingham, UK.
Morrissey
J
J
Williams
P
P
D002473:Cell Wall / Q000201:enzymology; D015964:Gene Expression Regulation, Bacterial; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006019:Glycolysis; D006801:Humans; D007501:Iron / Q000378:metabolism; D011990:Receptors, Transferrin / Q000378:metabolism*; D013203:Staphylococcal Infections / Q000382:microbiology; D013210:Staphylococcus / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D014774:Virulence
D011990:Receptors, Transferrin; D007501:Iron; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases