Search Results (2)

Background/Objectives: Melioidosis, caused by Burkholderia pseudomallei, is a severe tropical infectious disease associated with high mortality in endemic regions. Early diagnosis remains challenging because conventional diagnostic methods, including culture, serological assays, and molecular techniques, have limitations in sensitivity, specificity, processing time, and accessibility in resource-limited settings. This review evaluates current diagnostic approaches and highlights the potential of short peptide biomarkers for improving melioidosis detection. Methods: A narrative literature review was conducted using four electronic databases (PubMed, Scopus, Web of Science, and Google Scholar) covering publications from 2000 to 2024. Relevant studies were identified using predefined keywords related to melioidosis diagnostics, biomarkers, and peptide-based approaches, and were screened based on relevance to diagnostic methods and peptide biomarker development in Burkholderia pseudomallei. Results: Several biomarkers have been investigated for melioidosis diagnostics, including capsular polysaccharide (CPS), type III secretion system 1 (TTS1), and other virulence-associated proteins such as Hcp1 and BPSS1187. Among these, CPS and TTS1 are highly conserved and specific targets widely used in molecular and antigen-based detection methods. Short peptide epitopes derived from these antigens demonstrate promising advantages over whole proteins, including improved stability, high specificity, easier synthesis, and reduced production costs. Advances in epitope prediction technologies and peptide-based biosensors have further expanded the potential applications of short peptides in rapid diagnostic platforms, including ELISA, lateral flow immunoassays, and biosensor-based detection systems. Conclusions: Short peptide–based biomarkers represent a promising strategy for developing rapid, sensitive, and cost-effective diagnostic tools for melioidosis, particularly in endemic and resource-limited settings. Full article

Cystic fibrosis (CF) is a genetic disease due to mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. The most frequent mutation (p.Phe508del) results in a misfolded protein (p.Phe508del-CFTR) with an altered transport to the membrane of the cells via the conventional protein secretion (CPS) pathway. Nevertheless, it can use unconventional protein secretion (UPS). Indeed, p.Phe508del-CFTR forms a complex with GRASP55 to assist its direct trafficking from the endoplasmic reticulum to the plasma membrane. While GRASP55 is a key player of UPS, it is also a key player of stress-induced autophagy. In parallel, the unfolded protein response (UPR), which is activated in the presence of misfolded proteins, is tightly linked to UPS and autophagy through the key effectors IRE1, PERK, and ATF6. A better understanding of how UPS, UPR, and stress-induced autophagy interact to manage protein trafficking in CF and other conditions could lead to novel therapeutic strategies. By enhancing or modulating these pathways, it may be possible to increase p.Phe508del-CFTR surface expression. In summary, this review highlights the critical roles of UPS- and UPR-induced autophagy in managing protein transport, offering new perspectives for therapeutic approaches. Full article