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Background Coxiella burnetii , an intracellular pathogen, serves as the causative agent of zoonotic Q fever. This pathogen presents a significant threat due to its potential for airborne transmission, environmental persistence, and pathogenicity. The current whole-cell vaccine (WCV) utilized in Australia to combat Q fever exhibits notable limitations, including severe adverse reactions and limited regulatory approval for human use. This research employed the reverse vaccinology (RV) approach to uncover antigenic proteins and epitopes of C. burnetii , facilitating the development of more potent vaccine candidates. Methods The potential immunogenic proteins derived from C. burnetii RSA493/Nine Mile phase I (NMI) were extracted through manual, automated RV, and virulence factor database (VFDB) methods. Web tools and bioinformatics were used to evaluate physiochemical attributes, subcellular localization, antigenicity, allergenicity, human homology, B-cell epitopes, MHC I and II binding ratios, functional class scores, adhesion probabilities, protein-protein interactions, and molecular docking. Results Out of the 1850 proteins encoded by RSA493/NMI, a subset of 178 demonstrated the potential for surface or membrane localization. Following a series of analytical iterations, 14 putative immunogenic proteins emerged. This collection included nine proteins (57.1%) intricately involved in cell wall/membrane/envelope biogenesis processes (CBU_0197 (Q83EW1), CBU_0311 (Q83EK8), CBU_0489 (Q83E43), CBU_0939 (Q83D08), CBU_1190 (P39917), CBU_1829 (Q83AQ2), CBU_1412 (Q83BU0), CBU_1414 (Q83BT8), and CBU_1600 (Q83BB2)). The CBU_1627 (Q83B86 ) (7.1%) implicated in intracellular trafficking, secretion, and vesicular transport, and CBU_0092 (Q83F57) (7.1%) contributing to cell division. Additionally, three proteins (21.4%) displayed uncharacterized functions (CBU_0736 (Q83DJ4), CBU_1095 (Q83CL9), and CBU_2079 (Q83A32)). The congruent results obtained from molecular docking and immune response stimulation lend support to the inclusion of all 14 putative proteins as potential vaccine candidates. Notably, seven proteins with well-defined functions stand out among these candidates. Conclusions The outcomes of this study introduce promising proteins and epitopes for the forthcoming formulation of subunit vaccines against Q fever, with a primary emphasis on cellular processes and the virulence factors of C. burnetii .

Background Emergence of new variants mainly variants of concerns (VOC) is caused by mutations in main structural proteins of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Therefore, we aimed to investigate the mutations among structural proteins of SARS-CoV-2 globally. Methods We analyzed samples of amino-acid sequences (AASs) for envelope (E), membrane (M), nucleocapsid (N), and spike (S) proteins from the declaration of the coronavirus 2019 (COVID-19) as pandemic to January 2022. The presence and location of mutations were then investigated by aligning the sequences to the reference sequence and categorizing them based on frequency and continent. Finally, the related human genes with the viral structural genes were discovered, and their interactions were reported. Results The results indicated that the most relative mutations among the E, M, N, and S AASs occurred in the regions of 7 to 14, 66 to 88, 164 to 205, and 508 to 635 AAs, respectively. The most frequent mutations in E, M, N, and S proteins were T9I, I82T, R203M/R203K, and D614G. D614G was the most frequent mutation in all six geographical areas. Following D614G, L18F, A222V, E484K, and N501Y, respectively, were ranked as the most frequent mutations in S protein globally. Besides, A-kinase Anchoring Protein 8 Like (AKAP8L) was shown as the linkage unit between M, E, and E cluster genes. Conclusion Screening the structural protein mutations can help scientists introduce better drug and vaccine development strategies.

Background Recent advancements in the management of pediatric liver trauma have highlighted the effectiveness of non-operative management as the preferred therapeutic approach. This report presents the case of an 8-year-old patient who sustained significant liver trauma from a substantial fall, successfully managed through non-operative management. Case presentation An 8-year-old Iranian child presented with a Grade IV liver laceration and contusion, pneumothorax, and rib fractures after a 1.5 m fall. Initial stable vitals were confirmed. Diagnostic evaluations included serial focused assessment with sonography for trauma scans and computed tomography imaging of the thorax, abdomen, and pelvis. Treatment involved intensive care unit monitoring, intravenous fluid therapy, and a chest tube insertion. The patient’s condition improved significantly after 6 days in the intensive care unit, demonstrating the efficacy of non-operative management. The patient was successfully discharged following conservative management. Written informed consent was obtained from the patient’s legal guardian for publication of this case report and any accompanying images. Conclusions This case highlights the effectiveness of non-operative management in managing high-grade liver injuries. Over the past 2 decades, non-operative management has become increasingly prevalent, particularly in urban healthcare settings, due to its ability to manage hepatic trauma without surgical risks. Advanced imaging and multidisciplinary approaches are critical to its success.

Some bacterial species within the Enterobacteriaceae family possess different types of fimbrial (pili) adhesins that promote adherence to cells and colonization of host tissues. One of the well-characterized fimbrial systems is the pap operon, which encodes P fimbriae, a key virulence factor in urinary and systemic infections. One of the key regulators of P fimbriae is the transcriptional regulator PapB which plays a pivotal role as a master switch, not only by directing phase-variable expression of its own operon but also by influencing expression of heterologous fimbrial systems. This review explores the structural organization, biogenesis, and multi-tiered regulatory control of P fimbriae, with emphasis on PapB and homologous regulatory proteins such as SfaB, FocB, PixB, and PefB. Comparative genomics and phylogenetic analyses reveal that regulators belonging to the PapB family are evolutionarily conserved across π-fimbrial systems and also regulate other types of fimbriae. These regulators respond to epigenetic changes, host-derived signals, and global transcriptional cues to control levels of production of specific fimbriae in a bacterial population to dynamically modulate bacterial adhesion in different environmental niches. Optimally, understanding these mechanisms could lead to novel approaches to perturb PapB-family proteins and abrogate production of some types of fimbriae as a targeted strategy to prevent bacterial infections dependent on adherence mediated by PapB family regulators.

Heteroresiatnce (HR) is the type of resistance toward one or more antibiotics appearing as a population of the bacterial load consisting of one or more subpopulations with lower antibiotic susceptibility levels than others. Due to the lack of appropriate diagnosis of HR isolates and their importance in resistance emergence to antibiotics, investigating the origins, emergence factors, and HR inhibitors is critical in combating antibiotic resistance. Efflux pumps (EPs) are bacterial systems that own an influential role in acquiring resistance toward anti-bacterial compounds. Studies on EPs revealed that they can affect HR emergence mechanisms and are competent to be introduced as a suitable bacterial target for diagnostic and therapeutic development in combating HR isolates. This review will consider the relations between EPs and the emergence of HR isolates and discuss their importance in confronting this type of antibiotic resistance.

To address a highly mutable pathogen, mutations must be evaluated. SARS-CoV-2 involves changing infectivity, mortality, and treatment and vaccination susceptibility resulting from mutations. We investigated the Asian and worldwide samples of amino-acid sequences (AASs) for envelope (E), membrane (M), nucleocapsid (N), and spike (S) proteins from the announcement of the new coronavirus 2019 (COVID-19) up to January 2022. Sequence alignment to the Wuhan-2019 virus permits tracking mutations in Asian and global samples. Furthermore, we explored the evolutionary tendencies of structural protein mutations and compared the results between Asia and the globe. The mutation analyses indicated that 5.81%, 70.63%, 26.59%, and 3.36% of Asian S, E, M, and N samples did not display any mutation. Additionally, the most relative mutations among the S, E, M, and N AASs occurred in the regions of 508 to 635 AA, 7 to 14 AA, 66 to 88 AA, and 164 to 205 AA in both Asian and total samples. D614G, T9I, I82T, and R203M were inferred as the most frequent mutations in S, E, M, and N AASs. Timeline research showed that substitution mutation in the location of 614 among Asian and total S AASs was detected from January 2020. N protein was the most non-conserved protein, and the most prevalent mutations in S, E, M, and N AASs were D614G, T9I, I82T, and R203M. Screening structural protein mutations is a robust approach for developing drugs, vaccines, and more specific diagnostic tools.

can cause several infections. Its capability to form biofilm has been reported to be a vital property involved in the bacteria's pathogenesis. Various genes contributing to biofilm formation have not yet been completely clarified. This study was designed to evaluate the factors influencing adherence and biofilm formation in isolated from paediatric patients. One hundred and ninety-seven isolates were obtained from pediatric patients and confirmed with phenotypic and molecular examinations. Antimicrobial susceptibility testing and biofilm formation were evaluated using standard methods. The genes encoding adhesion and virulence factors were investigated by the PCR method. The most efficient antibiotics against isolates were vancomycin and linezolid. Approximately, 54.2% of MSSA and 85.6% of MRSA isolates were biofilm producers according to the microtiter test. Our analysis indicated that MRSA isolates are better able to form biofilm compared with MSSA isolates. All isolates harbored , and , while , and were detected in 99.5%, 42.1%, 97.5%, and 5.6% of isolates, respectively. In addition, a significant difference was found in gene and biofilm formation. Our findings showed a significant correlation between and genes and MRSA and biofilm formation in isolates. Additionally, this study indicated the significant role of the gene as a major marker for S. aureus biofilm formation. Therefore, further experiments are warranted to exactly elucidate the function of the gene in the formation of biofilm.

Emergence of new variants mainly variants of concerns (VOC) is caused by mutations in main structural proteins of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Therefore, we aimed to investigate the mutations among structural proteins of SARS-CoV-2 globally. We analyzed samples of amino-acid sequences (AASs) for envelope (E), membrane (M), nucleocapsid (N), and spike (S) proteins from the declaration of the coronavirus 2019 (COVID-19) as pandemic to January 2022. The presence and location of mutations were then investigated by aligning the sequences to the reference sequence and categorizing them based on frequency and continent. Finally, the related human genes with the viral structural genes were discovered, and their interactions were reported. The results indicated that the most relative mutations among the E, M, N, and S AASs occurred in the regions of 7 to 14, 66 to 88, 164 to 205, and 508 to 635 AAs, respectively. The most frequent mutations in E, M, N, and S proteins were T9I, I82T, R203M/R203K, and D614G. D614G was the most frequent mutation in all six geographical areas. Following D614G, L18F, A222V, E484K, and N501Y, respectively, were ranked as the most frequent mutations in S protein globally. Besides, A-kinase Anchoring Protein 8 Like (AKAP8L) was shown as the linkage unit between M, E, and E cluster genes. Screening the structural protein mutations can help scientists introduce better drug and vaccine development strategies.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a new member of the Coronaviridae family, triggering more than 190 million cases and more than two million deaths in European societies. Emerging the new variants due to mutations in genomic regions are foremost responsible for influencing the infectivity and mortality potential of such a virus. In the current study, we considered mutations among spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins of SARS-CoV-2 in the Europe continent by exploring the frequencies of mutations and the timeline of emerging them. For this purpose, Amino-acid sequences (AASs) were gathered from the GISAID database, and Mutation tracking was performed by detecting any difference between samples and a reference sequence; Wuhan-2019. In the next step, we compared the achieved results with worldwide sequences. 8.6%, 63.6%, 24.7%, and 1.7% of S, E, M, and N samples did not demonstrate any mutation among European countries. Also, the regions of 508 to 635 AA, 7 to 14 AA, 66 to 88 AA, and 164 to 205 AA in S, E, M, and N samples contained the most mutations relative to the total AASs in both Europe AASs and worldwide samples. D614G, A222V, S477N, and L18F were the first to fifth frequent mutations in S AASs among European samples, and T9I, I82T, and R203M were the first frequent mutations among E, M, and S AASs of the Europe continent. Investigating the mutations among structural proteins of SARS-CoV-2 can improve the strength of therapeutic and diagnostic strategies to efficient combat the virus and even maybe efficient in predicting new emerging variants of concern. Competing Interest Statement The authors have declared no competing interest.