Intellectual Profile and Intolerance of Uncertainty in Adults with High-Functioning Autism

Исследован профиль интеллектуальных способностей и личностные особенности у взрослых социально адаптированных пациентов с расстройствами аутистического спектра (РАС). Испытуемые прошли процедуру тестирования интеллекта с помощью теста Векслера (WAIS-III), заполнили опросники толерантности к неопределенности (НОТН) и коэффициент аутизма (AQ). Для пациентов с РАС было характерно статистически достоверное снижение вербального интеллекта и аномально повышенный уровень нетерпимости к неопределенности в сравнении с нейротипичными добровольцами того же пола и возраста. Дефицит социальных навыков у пациентов с РАС прямо коррелировал со снижением вербальной гибкости, но не с их отношением к неопределенности.We assessed the profile of intellectual abilities and personal traits in high-functioning adults with autism spectrum disorders (ASD). We used the standard Wechsler Test (WAIS-III) of intelligence quotient and two questionnaires — Autism quotient (AQ) and the New questionnaire for tolerance to uncertainty. In contrast with age-matched neurotypical controls, patients with ASD demonstrated moderate deficit only in the verbal domain of intellectual abilities and abnormal intolerance to uncertainty. Self-reported difficulties in social interaction in patients with ASD was positively correlated with a low verbal flexibility, but not with their personal attitudes to uncertainty.Исследование выполнено при поддержке Российского научного фонда, грант № 20-18-0025

AglH, a thermophilic UDP‑<i>N</i>‑acetylglucosamine‑1‑phosphate:dolichyl phosphate GlcNAc‑1‑phosphotransferase initiating protein<i> N</i>‑glycosylation pathway in <i>Sulfolobus acidocaldarius</i>, is capable of complementing the eukaryal Alg7

AglH, a predicted UDP-GlcNAc-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase, is initiating the protein N-glycosylation pathway in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. AglH successfully replaced the endogenous GlcNAc-1-phosphotransferase activity of Alg7 in a conditional lethal Saccharomyces cerevisiae strain, in which the first step of the eukaryal protein N-glycosylation process was repressed. This study is one of the few examples of cross-domain complementation demonstrating a conserved polyprenyl phosphate transferase reaction within the eukaryal and archaeal domain like it was demonstrated for Methanococcus voltae (Shams-Eldin et al. 2008). The topology prediction and the alignment of the AglH membrane protein with GlcNAc-1-phosphotransferases from the three domains of life show significant conservation of amino acids within the different proposed cytoplasmic loops. Alanine mutations of selected conserved amino acids in the putative cytoplasmic loops II (D(100)), IV (F(220)) and V (F(264)) demonstrated the importance of these amino acids for cross-domain AlgH activity in in vitro complementation assays in S. cerevisiae. Furthermore, antibiotic treatment interfering directly with the activity of dolichyl phosphate GlcNAc-1-phosphotransferases confirmed the essentiality of N-glycosylation for cell survival