Molecular Biology: Open Access

Exosomes are extracellular vesicles that play crucial roles in intercellular communication by transporting various biomolecules, including microRNAs (miRNAs). In the context of HIV infection, exosomes derived from infected cells, particularly macrophages, have gained attention for their potential role in viral pathogenesis and immune modulation. This review focuses on exosomal microRNAs derived from HIV-infected macrophages, exploring their biogenesis, composition, functional roles in viral persistence and immune evasion and potential as biomarkers or therapeutic targets. Understanding the interplay between exosomal miRNAs and HIV pathogenesis can provide insights into novel strategies for disease management and therapeutic intervention.

Intranasal exposure to ricin, a potent plant-derived toxin, leads to diverse interactions between ricin and pulmonary cells, impacting respiratory health and systemic toxicity. This review explores the multifaceted interactions of ricin with cells in the pulmonary system, encompassing mechanisms of uptake, intracellular trafficking, cytotoxic effects and immune responses. Understanding these interactions is crucial for developing effective therapeutic strategies and mitigating the harmful effects of ricin exposure on respiratory function and overall health.

Rift Valley Fever Virus (RVFV) is a significant pathogen known for causing severe febrile illness and hemorrhagic fever in humans and substantial economic losses in livestock. The virus is a member of the Phlebovirus genus in the Bunyaviridae family, with a segmented RNA genome that encodes essential proteins for viral replication and transcription. Among these, the L protein is a critical component of the viral RNA polymerase complex, responsible for synthesizing viral RNA. Despite its pivotal role, the detailed tertiary structure of the L protein remains poorly characterized. The primary objective of this study is to elucidate the tertiary structure of the RVFV L protein using a combination of structural biology techniques. By understanding the spatial arrangement of this protein, we aim to uncover its functional mechanisms and identify potential targets for therapeutic intervention. A multi-faceted approach was employed, integrating bioinformatics, molecular modeling, X-ray crystallography and cryo-Electron Microscopy (cryo-EM). Computational tools were used to predict structural features, while experimental methods provided highresolution structural data. Structural models were validated through comparisons with homologous proteins and functional assays to ascertain their biological relevance.

Alzheimer's disease is a progressive neurodegenerative disorder that affects millions of people worldwide. The disease is characterized by the accumulation of amyloid-beta plaques and neurofibrillary tangles in the brain, which lead to the loss of neurons and cognitive decline. While the exact causes of Alzheimer's disease are not fully understood, recent research has shed light on the molecular biology and genetics underlying the disease. One of the key molecular features of Alzheimer's disease is the accumulation of plaques in the brain. Peptide that is produced through the cleavage of the Amyloid Precursor Protein (APP) by the enzymes. In healthy individuals, brain through a variety of mechanisms, including enzymatic degradation and clearance by immune cells. However, in Alzheimer's disease, accumulates in the brain, forming plaques that are toxic to neurons.