PrionDB: Extraction of mutation data from the literature

2005, PrionDB.

This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation M204S was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation M204S in PRIO_MOUSE

Point mutation:	M204S
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_MOUSE (Prnp,Prn-p)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in PRIO_MOUSE
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 205 in Mammalian prion proteins family Position 205 in Prion proteins (PRP, PRNP) family
Reference:	Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor. Kiachopoulos S, Bracher A, Winklhofer KF, Tatzelt J J Biol Chem 2005 Mar 11;280(10):9320-9. Epub 2004 Dec 10.	Medline
Other point mutations / same article	List
Text source	HTML and PDF full texts
Validation status	True positive

Relevant sentences:

M204S

PrP-M204S was described earlier (19 )
Notably , in both assays the phenotype of T182A was similar to M204S , a PrP mutant generated and characterized in a previous study from our group (19 )
The single amino acid substitution in M204S destabilizes an interaction of helix 3 with helix 1
As a consequence , M204S does not receive a GPI anchor , the core glycans are not converted into complex structures , and the mutant protein is secreted into the cell culture medium (19 )
N2a cells were transiently transfected either with wild type PrP (wt) , with PrP mutants lacking the first glycosylation site (N180Q and T182A) , or with PrP-M204S , a mutant with a disrupted hydrophobic interaction between helix 3 and helix 1 (19 )
Similarly , high mannose glycoforms of different PrP mutants , such as M204S , are efficiently secreted (19 )
Neither WT PrP nor the monoglycosylated mutant N180Q was present in the cell extracts , however , the T182A mutant could be detected in the detergent-insoluble fraction of the heterologous cells , similarly to M204S , which is efficiently secreted as well (19 )
Cell culture medium collected from cells transiently transfected with WT PrP , M204S , N180Q , and T182A was filtered and added to untransfected N2a cells
As predicted , V160S , V160W , and M204S severely affected the maturation of PrP , similarly to the pathogenic mutations T182A and F197S
The single amino acid substitution in M204S destabilizes an interaction of helix -->with helix 1
Misfolding of Mutant Prion Protein9322 high mannose glycoforms of different PrP mutants , such as M204S , are efficiently secreted (19)
N2a cells were transiently transfected either with wild type PrP (wt) , with PrP mutants lacking the first glycosylation site (N180Q and T182A) , or with PrP-M204S , a mutant with a disrupted hydrophobic interaction between helix -->and helix 1 (19)

F.Horn (priondbcmbi.ru.nl), 22-Aug-2005