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Literature summary for 3.4.21.112 extracted from

  • Maisa, A.; Stroeher, U.; Klenk, H.D.; Garten, W.; Strecker, T.
    Inhibition of Lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants (2009), PLoS Negl. Trop. Dis., 3, e446.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.112

Application

Application Comment Organism
medicine glycoprotein cleavage by S1P is a promising target for the development of novel anti-arenaviral strategies Cricetulus griseus

Protein Variants

Protein Variants Comment Organism
additional information stable cell lines inducibly expressing S1P-adapted alpha1-antitrypsin variants inhibit the proteolytic maturation of glycoprotein GP-C. Introduction of the S1P recognition motifs RRIL and RRLL into the reactive center loop of alpha1-antitrypsin results in abrogation of glycoprotein GP-C processing by endogenous S1P to a similar level observed in S1P-deficient cells. Moreover, S1P-specific alpha1-antitrypsins significantly inhibit replication and spread of a replication-competent recombinant vesicular stomatitis virus expressing the Lassa virus glycoprotein GP as well as authentic Lassa virus Cricetulus griseus

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Cricetulus griseus Q9Z2A8
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-

Source Tissue

Source Tissue Comment Organism Textmining
CHO cell
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 Cricetulus griseus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycoprotein precursor Gc + H2O
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 Cricetulus griseus ?
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 ?

Synonyms

Synonyms Comment Organism
convertase site 1 protease
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 Cricetulus griseus
S1P
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 Cricetulus griseus

General Information

General Information Comment Organism
malfunction in CHO cells deficient of S1P (termed SRD-12B cells) glycoprotein GP-C processing is abrogated after Lassa virus infection Cricetulus griseus