Ali Rohman

Background/Objectives: Ventricular septal defect (VSD) is the most common congenital heart disease in children and is often associated with growth impairment and malnutrition. Increased metabolic demand, feeding difficulties, and recurrent infections contribute to poor nutritional status. Insulin-like growth factor-1 (IGF-1), a key mediator of growth hormone activity, reflects nutritional and metabolic conditions. Previous studies have evaluated endocrine and growth abnormalities in heterogeneous congenital heart disease populations. However, data specifically examining the relationship between serum IGF-1 levels and nutritional status in isolated pediatric ventricular septal defect remain limited, particularly in Southeast Asian populations. Methods: The single centre observational case–control study was conducted at Dr. Soetomo Hospital, Surabaya, involving 110 children (55 VSD patients and 55 healthy controls). VSD diagnosis was confirmed by echocardiography. Nutritional status was assessed using WHO anthropometric criteria. Serum IGF-1 levels were measured using ELISA. Statistical analyses compared IGF-1 levels between groups and across nutritional categories. Results: Moderate and severe wasting were more common in the VSD group. Median IGF-1 levels were significantly lower in VSD patients compared to controls (5.18 vs. 21.4 ng/mL; p < 0.001). A positive association between IGF-1 levels and nutritional status was observed. Conclusions: Children with VSD have poorer nutritional status and significantly lower IGF-1 levels compared to healthy controls. This association may be explained by the dysregulation of the growth hormone–IGF-1 axis. IGF-1 may complement nutritional assessment for identifying and monitoring growth impairment and guiding early nutritional interventions in pediatric VSD.

Congenital heart disease (CHD) represents nearly one-third of congenital birth defects annually, with ventricular septal defect (VSD) being the most common type. The aim of this study was to explore the role of specific GATA binding protein 6 gene (GATA6) mutations as a potential etiological factor in the development of VSD through an in silico approach. Data were collected from the human gene databases: DisGeNET and GeneCards, with protein-protein interaction networks constructed via STRING and Cytoscape. Gene ontology and pathway enrichment analyses were conducted using DAVID, with data analysis in R with significance set at FDR p<0.05. Target single nucleotide polymorphisms (SNPs) of GATA6 were obtained from NCBI dbSNP, and non-synonymous single nucleotide polymorphism (nsSNP) effects were predicted using SIFT, PolyPhen-2, I-Mutant 2.0, Fathmm, MutPred 2.0, SNP&GO, and PON-P2. Conserved regions of GATA6 were analyzed using ConSurf, with functional classification, variant conservation, and stability changes evaluated in Google Colab. Multiple sequence alignment was performed using ClustalW. Mutation modeling and molecular dynamics analysis, using GROMACS, revealed that among 87 intersecting genes, 16 proteins were interconnected with GATA6, showing a centrality value of 0.4378. Gene ontology analysis highlighted atrioventricular canal development, protein-DNA complexes, and transcription factor regulation as key processes for cardiac development, especially in the ventricular septum. NsSNP and molecular dynamics analyses identified rs387906818 and rs387906820 as having the highest pathogenic potential for VSD due to amino acid structural changes.

The severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) has spread globally and has led to extremely high mortality rates. In addition to infecting humans, this virus also has infected animals. Experimental studies and natural infections showed that dogs have a low susceptibility to SARS-CoV-2 infection, whereas domesticated cats and other animals in the family Felidae, such as lions, tigers, snow leopards, and cougars, have a high susceptibility to viral infections. In addition, wild white-tailed deer, gorillas, and otters have been found to be infected by SARS-CoV-2. Furry farm animals, such as minks, have a high susceptibility to SARS-CoV-2 infection. The virus appears to spread among minks and generate several new mutations, resulting in increased viral virulence. Furthermore, livestock animals, such as cattle, sheep, and pigs, were found to have low susceptibility to the virus, whereas chicken, ducks, turkeys, quail, and geese did not show susceptibility to SARS-CoV-2 infection. This knowledge can provide insights for the development of SARS-CoV-2 mitigation strategies in animals and humans. Therefore, this review focuses on experimental (both replication and transmission) in vitro, ex vivo, and in vivo studies of SARS-CoV-2 infections in pets and in wild and farm animals, and to provide details on the mechanism associated with natural infection.

Outbreaks of dengue virus (DENV) in Indonesia have been mainly caused by the DENV serotype-1; -2; or -3. The DENV-4 was the least-reported serotype in Indonesia during the last five decades. We recently conducted a molecular epidemiology study of dengue in the Jember regency, East Java province, Indonesia. Dengue is endemic in the region and outbreaks occur annually. We investigated the clinical characteristics and etiology of dengue-like febrile illness in this regency to understand the disease dynamics. A total of 191 patients with clinical symptoms similar to dengue were recruited during an 11-month study in 2019–2020. Children accounted for the majority of cases and dengue burden was estimated in 41.4% of the cases based on NS1 antigen, viral RNA, and IgG/IgM antibody detection with the majority (73.4%) being primary infections. Secondary infection was significantly associated with a higher risk of severe dengue manifestation. All four DENV serotypes were detected in Jember. Strikingly, we observed the predominance of DENV-4, followed by DENV-3, DENV-1, and DENV-2. Genotype determination using Envelope gene sequence revealed the classification into Genotype I, Cosmopolitan Genotype, Genotype I, and Genotype II for DENV-1, -2, -3, and -4, respectively. The predominance of DENV-4 in Jember may be associated with a new wave of DENV infections and spread in a non-immune population lacking a herd-immunity to this particular serotype.

Xylan, a prominent component of cellulosic biomass, has a high potential for degradation into reducing sugars, and subsequent conversion into bioethanol. This process requires a range of xylanolytic enzymes. Among them, β-xylosidases are crucial, because they hydrolyze more glycosidic bonds than any of the other xylanolytic enzymes. They also enhance the efficiency of the process by degrading xylooligosaccharides, which are potent inhibitors of other hemicellulose-/xylan-converting enzymes. On the other hand, the β-xylosidase itself is also inhibited by monosaccharides that may be generated in high concentrations during the saccharification process. Structurally, β-xylosidases are diverse enzymes with different substrate specificities and enzyme mechanisms. Here, we review the structural diversity and catalytic mechanisms of β-xylosidases, and discuss their inhibition by monosaccharides.

Complete degradation of the xylan backbone of hemicellulosic plant cell walls requires the synergistic action of endo-xylanases and β-1,4-xylosidases. While endo-xylanases produce xylooligosaccharides from xylan, β-1,4-xylosidases degrade the xylooligosaccharides into xylose monomers. The glycoside hydrolase family 43 β-1,4-xylosidase from Geobacillus thermoleovorans IT-08 is a promising, heat stable catalyst for the saccharification of hemicellulosic material into simple fermentable sugars, but it is competitively inhibited by its products arabinose and xylose. As a first step to help overcome this problem, we elucidated crystal structures of the enzyme in the unliganded form and with bound products, at 1.7–2.0 Å resolution. The structures are very similar to those of other enzymes belonging to glycoside hydrolase family 43. Unexpectedly, the monosaccharides are bound in very different ways. Arabinose preferentially binds in subsite -1, while xylose exclusively interacts with subsite +1. These structures and sugar binding preferences suggest ways for improving the catalytic performance of the enzyme by rational mutational design.