Biology subjects

Tijani, M.

Publications and source records attributed to Tijani, M..

4 recordsLinked to original sources

bioRxiv2020

A Cross-Sectional Study of the Prevalence and Risk Factors of Soil Transmitted Helminthes Infection and Stunting Among School-aged Children in Ibadan

BackgroundIn developing countries, infections caused by soil-transmitted helminthes (STH), such as Ascaris, Trichuris and hookworm, pose major public health problems among the school-age children, resulting in impaired physical growth such as stunting and thinness, and cognitive development. The aim of this study is to determine the prevalence of STH infections, stunting and thinness, and risk factors among school-age-children in Ibadan. This becomes highly imperative in order to serve as a guide on the prevention and control. MethodA cross-sectional study was carried out in 8 primary schools at Ibadan, Oyo State Nigeria, between May and November 2018. All the school-age-children between the ages 5 and 18 years old (mean 10.4 {+/-} 1.7 years), from primary one to six took part in the study. Demographic data were obtained and STH infections was analysed in single-stool samples by Kato-Katz. Anthropometric parameters were taken to calculate Height for-age Z score (HAZ) and Body-Mass-Index (BMI) for-age Z score (BAZ), in order to determine among school-aged-children stunting and thinness respectively. ResultsIn overall, 458 school-age-children partook in the study. The prevalence of STH was 9.0%, out of which 7.6%, 2.8% and 1.5% were recorded for Ascaris, Trichuris and multiparasitism respectively. The overall prevalence obtained revealed that the results of stunting and thinness (HAZ < -2SD, BAZ < -2SD) were 24.7% and 27.3% respectively based on the WHO Child Growth Standards (2007). Notably, ages of the children (P< 0.01), their classes (P=0.05), different schools (P=0.003), washing of hands after toileting (P = 0.05) were important risk factors determining STH infection, HAZ and BAZ. ConclusionThe study showed that specific risk factors among school children in the studied area will make them vulnerable with high risk of STH infection, HAZ and BAZ. Effective prevention and control strategies can be well planned when risk factors and dynamics of transmission in vulnerable groups have been painstakingly identified. SummaryAscaris, Trichuris and hookworm are responsible for major public health problems among the school-age children (SAC); this has led to stunting and thinness, and impaired cognitive development. With the aim to determine prevalence of STH infections, stunting, thinness and associated risk factors, a cross-sectional study of STH infection in 8 primary schools at Ibadan, Oyo State Nigeria was conducted in 2018. School-aged children between the ages of 5 and 18 were enrolled, demographic data, stool samples and anthropometric parameters were obtained in order to determine STH infection and nutritional status. 9.0% was the prevalence of STH, the prevalence of 7.6%, 2.8% and 1.5% were recorded for Ascaris, Trichuris and multiparasitism respectively, while 24.7% and 27.3% were obtained for stunting and thinness respectively. The childrens age, hand washing after toileting and locations of the different schools were significantly correlated with STH infection, HAZ and BAZ. This study is highly imperative because its shows some risk factors associated with STH infection, HAZ and BAZ among SAC, this can serve as a guide on the prevention and control among SAC.

molecular biology↗

bioRxiv2019

Role for Merlin/NF2 in transcription elongation through interaction with the PAF complex

The PAF complex (PAFC) coordinates transcription elongation and mRNA processing events and its CDC73/parafibromin subunit functions as a tumour suppressor. The NF2/Merlin tumour suppressor functions at the cell cortex and nucleus and is a key mediator of contact inhibition. Here we provide a direct link between nuclear Merlin and transcription elongation controlled by cell-cell adhesion. Merlin interacts with the PAFC in a cell density-dependent manner and tumour-derived inactivating mutations in both Merlin and CDC73 mutually disrupt their interaction. Growth suppression by Merlin requires CDC73 and Merlin regulates PAFC association with chromatin in a subset of genes. We also identify by CDC73 affinity-proteomics a role for FAT cadherins in regulating the Merlin-PAFC interaction. Our results suggest that in addition to its function within the Hippo pathway, nuclear Merlin is part of a tumour suppressor network which coordinates postinitiation steps of the transcription cycle of genes mediating in contact inhibition.

cancer biology↗

bioRxiv2018

Characterisation of Antibody Interactions with the G Protein of Vesicular Stomatitis Virus Indiana Strain and Other Vesiculovirus G Proteins

Vesicular stomatitis virus Indiana strain G protein (VSVind.G) is the most commonly used envelope glycoprotein to pseudotype lentiviral vectors (LV) for experimental and clinical applications. Recently, G proteins derived from other vesiculoviruses (VesG), for example Cocal virus, have been proposed as alternative LV envelopes with possible advantages compared to VSVind.G. Well-characterised antibodies that recognise VesG will be useful for vesiculovirus research, development of G protein-containing advanced therapy medicinal products (ATMPs), and deployment of VSVind-based vaccine vectors. Here we show that one commercially available monoclonal antibody, 8G5F11, binds to and neutralises G proteins from three strains of VSV as well as Cocal, and Maraba viruses, whereas the other commercially available monoclonal anti-VSVind.G antibody, IE9F9, binds to and neutralises only VSVind.G. Using a combination of G protein chimeras and site-directed mutations, we mapped the binding epitopes of IE9F9 and 8G5F11 on VSVind.G. IE9F9 binds close to the receptor binding site and competes with soluble low-density lipoprotein receptor (LDLR) for binding to VSVind.G, explaining its mechanism of neutralisation. In contrast, 8G5F11 binds close to a region known to undergo conformational changes when the G protein moves to its post-fusion structure, and we propose that 8G5F11 cross-neutralises VesGs by inhibiting this.\n\nIMPORTANCEVSVind.G is currently regarded as the gold-standard envelope to pseudotype lentiviral vectors. However, recently other G proteins derived from vesiculoviruses have been proposed as alternative envelopes. Here, we investigated two anti-VSVind.G monoclonal antibodies for their ability to cross-react with other vesiculovirus G proteins, and identified the epitopes they recognise, and explored the mechanisms behind their neutralisation activity. Understanding how cross-neutralising antibodies interact with other G proteins may be of interest in the context of host-pathogen interaction and co-evolution as well as providing the opportunity to modify the G proteins and improve G protein-containing medicinal products and vaccine vectors.

microbiology↗

bioRxiv2018

TMEM16F activation by Ca2+ triggers plasmalemma expansion and directs PD-1 trafficking

TMEM16F, an ion channel gated by high cytoplasmic Ca2+, is required for cell surface phosphatidylserine exposure during platelet aggregation and T cell activation. Here we demonstrate in Jurkat T cells and HEK293 cells that TMEM16F activation triggers large-scale surface membrane expansion in parallel with lipid scrambling. Following TMEM16F mediated scrambling and surface expansion, cells undergo extensive membrane shedding. The membrane compartment that expands the cell surface does not involve endoplasmic reticulum or acidified lysosomes. Surprisingly, T cells lacking TMEM16F expression not only fail to expand surface membrane, but instead rapidly internalize membrane via massive endocytosis (MEND). The T cell co-receptor PD-1 is selectively shed when TMEM16F triggers membrane expansion, while it is selectively internalized in the absence of TMEM16F. Its participation in this trafficking is determined by its single transmembrane domain. Thus, we establish a fundamental role for TMEM16F as a regulator of Ca2+-activated membrane trafficking.

cell biology↗