Adjectives in Thai: Implications for a functionalist typology of word classes

Tai languages are often described as “lacking” a major lexical class “adjectives”; accordingly, they and other area languages are frequently cited as evidence against adjectival universality. This article brings the putative lack under examination, arguing that a more complete distributional analysis reveals a pattern: overlap is highest among semantically peripheral adjectives and verbs and in constructions prototypically associated to both classes crosslinguistically, and lowest among semantically core adjectives and verbs and in constructions prototypically associated to only one or the other class. Rather than “lacking” adjectives, data from Thai thus in fact support functional-typological characterizations of adjectival universality such as those of Givón (1984), Croft (2001), and Dixon (2004). Finally, while data from Thai would fail to falsify an adaptation of Enfield's (2004) Lao lexical class-taxonomy (in which adjectives are treated as a verbal subclass) on its own terms, this article argues that in absence of both universally-applicable criteria for the evaluation of categorial taxonomies crosslinguistically and evidence for the cognitive reality of categorial taxonomies so stipulated, even this more limited sense of a “lack” of adjectives in Thai is less radical a challenge to adjectival universality than has sometimes been supposed.

The N-terminal domain of Npro of classical swine fever virus determines its stability and regulates type I IFN production

The viral protein Npro is unique to the genus Pestivirus within the family Flaviviridae. After autocatalytic cleavage from the nascent polyprotein, Npro suppresses type I IFN (IFN-α/β) induction by mediating proteasomal degradation of IFN regulatory factor 3 (IRF-3). Previous studies found that the Npro-mediated IRF-3 degradation was dependent of a TRASH domain in the C-terminal half of Npro coordinating zinc by means of the amino acid residues C112, C134, D136 and C138. Interestingly, four classical swine fever virus (CSFV) isolates obtained from diseased pigs in Thailand in 1993 and 1998 did not suppress IFN-α/β induction despite the presence of an intact TRASH domain. Through systematic analyses, it was found that an amino acid mutation at position 40 or mutations at positions 17 and 61 in the N-terminal half of Npro of these four isolates were related to the lack of IRF-3-degrading activity. Restoring a histidine at position 40 or both a proline at position 17 and a lysine at position 61 based on the sequence of a functional Npro contributed to higher stability of the reconstructed Npro compared with the Npro from the Thai isolate. This led to enhanced interaction of Npro with IRF-3 along with its degradation by the proteasome. The results of the present study revealed that amino acid residues in the N-terminal domain of Npro are involved in the stability of Npro, in interaction of Npro with IRF-3 and subsequent degradation of IRF-3, leading to downregulation of IFN-α/β production.