Localized reversible frameshift mutation in an adhesin gene confers a phase-variable adherence phenotype in mycoplasma

The variable adherence-associated (Vaa) antigen of Mycoplasma hominis is an abundant surface lipoprotein adhesin that may mediate important interactions of this wall-less prokaryotic pathogen with the human host. Extensive mutational variation of Vaa size, as well as sequence and antigenic divergence, has been described previously. Using a series of clonal isolates representing an isogenic lineage of variants oscillating in Vaa expression, Vaa is further shown in this study to undergo high-frequency phase variation in expression, which correlated precisely with the ability of M . hominis to adhere to cultured human cells. Although no DNA rearrangements or sequence differences in the 5' regions flanking vaa alleles were detected between Vaa⁺ and Vaa⁻ variants, intragenic vaa sequences from this lineage revealed an oscillating mutation involving a single nucleotide deletion/insertion in a short tract of adenine residues near the 5' end of the mature Vaa coding sequence, which created a translational frameshift resulting in either a complete Vaa ORF or an in-frame UAG stop codon immediately downstream of the poly-A tract. Evidence for the occurrence of this high-frequency frameshift mutation in vivo was obtained from analysis of PCR-generated vaa sequences amplified from the joint synovial fluid of a patient with M . hominis -associated arthritis, which indicated that Vaa phase variation occurs during M . hominis infection in the natural host. These results identify a distinctive frameshift mutator element in the vaa gene that governs M . hominis adherence and highlight the importance of mutational alteration of primary gene products on the mycoplasma surface as a means of generating and maintaining functional diversity in the host.     

Perceptual Compensation Is Correlated with Individuals' “Autistic” Traits: Implications for Models of Sound Change

Variation is a ubiquitous feature of speech. Listeners must take into account context-induced variation to recover the interlocutor''s intended message. When listeners fail to normalize for context-induced variation properly, deviant percepts become seeds for new perceptual and production norms. In question is how deviant percepts accumulate in a systematic fashion to give rise to sound change (i.e., new pronunciation norms) within a given speech community. The present study investigated subjects'' classification of /s/ and // before /a/ or /u/ spoken by a male or a female voice. Building on modern cognitive theories of autism-spectrum condition, which see variation in autism-spectrum condition in terms of individual differences in cognitive processing style, we established a significant correlation between individuals'' normalization for phonetic context (i.e., whether the following vowel is /a/ or /u/) and talker voice variation (i.e., whether the talker is male or female) in speech and their “autistic” traits, as measured by the Autism Spectrum Quotient (AQ). In particular, our mixed-effect logistic regression models show that women with low AQ (i.e., the least “autistic”) do not normalize for phonetic coarticulation as much as men and high AQ women. This study provides first direct evidence that variability in human''s ability to compensate for context-induced variations in speech perceptually is governed by the individual''s sex and cognitive processing style. These findings lend support to the hypothesis that the systematic infusion of new linguistic variants (i.e., the deviant percepts) originate from a sub-segment of the speech community that consistently under-compensates for contextual variation in speech.     

Biosynthesis of man-β-G1cNAc-G1cNAc-pyrophosphoryl-polyprenol by a solubilized enzyme from aorta

The particulate enzyme fraction from pig aorta was treated with Triton X-100 or Nonidet P-40 to yield a soluble enzyme preparation. This solubilized enzyme catalyzed the transfer of mannose from GDP-[¹⁴C]mannose, but not from [¹⁴C]mannosyl-phosphoryl-polyprenol, to G1cNAc-G1cNAc-pyrophosphoryl-polyprenol to form the trisaccharide-lipid, Man-β-GlcNAc-GlcNAc-pyrophosphoryl-polyprenol. The trisaccharide-lipid formed in these reactions was isolated by solvent fractionation and was subjected to mild acid hydrolysis to release the [¹⁴C]trisaccharide. Essentially all of the radioactivity was released from this trisaccharide as mannose upon treatment with β-mannosidase while α-mannosidase had no effect.