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J. Biol. Chem., Vol. 275, Issue 37, 28569-28574, September 15, 2000
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From the Friedrich-Miescher Institut, CH-4058 Basel,
Switzerland
Properdin is the positive regulator of the
alternative pathway of complement activation. The 53-kDa protein is
essentially composed of six thrombospondin type 1 repeats, all
of which contain the WXXW motif, the recognition
sequence for C-mannosylation. C-Mannosylation
is a post-translational modification of tryptophan residues in which,
in contrast to the well known N- and
O-glycosylation, the carbohydrate is attached via a C-C
bond to C-2 of the indole moiety of tryptophan.
C-Mannosylation was first found in human RNase 2 and
interleukin-12. The terminal complement proteins C6-C9 also carry this
modification as part of their thrombospondin type 1 repeats. We studied
the C-mannosylation pattern of human properdin by mass
spectrometry and Edman degradation. Properdin contains 20 tryptophans
of which 17 are part of a WXXW motif. Fourteen tryptophans
were found to be modified 100%. This is the first example of a protein
in which the majority of tryptophan residues occurs in the
C-mannosylated form. These results show that
C-mannosylated proteins occur at several steps along the
complement activation cascade. Therefore, this system would be ideal to
investigate the function of C-mannosylation.
To whom correspondence should be addressed: Friedrich-Miescher
Institut, Maulbeerstr. 66, CH-4058 Basel, Switzerland. Tel.: 41-61-697-4531; Fax: 41-61-697-3976; E-mail:
Jan.Hofsteenge@fmi.ch.
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