Publications by authors named "R K Mallampalli"
Article Synopsis
- SARS-CoV-2 is evolving, resulting in new variants like XEC, which has specific mutations (T22N and F59S) in the spike protein that affect how the virus interacts with neutralizing antibodies.
- The study analyzed immune responses from different vaccinated groups and found that XEC had significantly lower neutralization levels due to the F59S mutation, but removing certain glycosylation sites could restore these levels.
- The research highlights that mutations in the N-terminal domain of the spike protein play a crucial role in the virus's ability to evade the immune system and change its structural properties.
Article Synopsis
- In the summer of 2024, a global increase in COVID-19 cases was attributed to JN.1 subvariants of SARS-CoV-2, which have new mutations, particularly in the spike protein's N-terminal domain (NTD).
- The study found that several subvariants (LB.1, KP.2.3, KP.3, and KP.3.1.1) largely escape neutralizing antibodies from various vaccines and past infections due to a key deletion (DelS31) in the spike protein.
- The DelS31 mutation enhances the stability of the spike protein and introduces changes that help the virus avoid immune detection, suggesting a possible need to update COVID-19 vaccines to include antigens
Introduction: The acute respiratory distress syndrome (ARDS) is a common complication of severe COVID-19 and contributes to patient morbidity and mortality. ARDS is a heterogeneous syndrome caused by various insults, and results in acute hypoxemic respiratory failure. Patients with ARDS from COVID-19 may represent a subgroup of ARDS patients with distinct molecular profiles that drive disease outcomes.
View Article and Find Full Text PDFThe severity of bacterial pneumonia can be worsened by impaired innate immunity resulting in ineffective pathogen clearance. We describe a mitochondrial protein, aspartyl-tRNA synthetase (DARS2), which is released in circulation during bacterial pneumonia in humans and displays intrinsic innate immune properties and cellular repair properties. DARS2 interacts with a bacterial-induced ubiquitin E3 ligase subunit, FBXO24, which targets the synthetase for ubiquitylation and degradation, a process that is inhibited by DARS2 acetylation.
View Article and Find Full Text PDFArticle Synopsis
- This study examines how subvariants of JN.1 (SLip, FLiRT, and KP.2) respond to neutralization by antibodies from vaccinated people and infected patients, discovering they show increased resistance compared to the original JN.1.
- The research finds that while hamster sera from XBB.1.5 vaccinations can strongly neutralize FLiRT and KP.2, SLip has reduced neutralization effectiveness. All subvariants demonstrate resistance to the antibody S309 and show decreased infectivity and other functionalities compared to JN.1.
- Key mutations in the spike protein of these subvariants are identified, affecting their interaction with antibodies and suggesting that new vaccines might need to