Bond PJ
Site-Specific Steric Control of SARS-CoV-2 Spike Glycosylation
A central tenet in the design of vaccines is the display of native-like antigens in the elicitation of protective immunity. The abundance of N-linked glycans across the SARS-CoV-2 spike protein is a potential source of heterogeneity among the many different vaccine candidates under investigation.
ReadThe antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase
Antibiotics that target Gram-negative bacteria in new ways are needed to resolve the antimicrobial resistance crisis1,2,3. Gram-negative bacteria are protected by an additional outer membrane, rendering proteins on the cell surface attractive drug targets4,5.
ReadAntibody affinity versus dengue morphology influences neutralization
Different strains within a dengue serotype (DENV1-4) can have smooth, or “bumpy” surface morphologies with different antigenic characteristics at average body temperature (37°C). We determined the neutralizing properties of a serotype cross-reactive human monoclonal antibody (HMAb) 1C19 for strains with differing morphologies within the DENV1 and DENV2 serotypes.
ReadSARS-CoV-2 S protein:ACE2 interaction reveals novel allosteric targets
The spike (S) protein is the main handle for SARS-CoV-2 to enter host cells via surface angiotensin-converting enzyme 2 (ACE2) receptors. How ACE2 binding activates proteolysis of S protein is unknown.
ReadSARS-CoV-2 Spike protein binds to bacterial lipopolysaccharide and boosts proinflammatory activity
There is a link between high lipopolysaccharide (LPS) levels in the blood and the metabolic syndrome, and metabolic syndrome predisposes patients to severe COVID-19. Here, we define an interaction between SARS-CoV-2 spike (S) protein and LPS, leading to aggravated inflammation *in vitro* and *in vivo*. Native gel electrophoresis demonstrated that SARS-CoV-2 S protein binds to LPS.
ReadThe Impact of Gag Non-Cleavage Site Mutations on HIV-1 Viral Fitness from Integrative Modelling and Simulations
The high mutation rate in retroviruses is one of the leading causes of drug resistance. In human immunodeficiency virus type-1 (HIV-1), synergistic mutations in its protease and the protease substrate – the Group-specific antigen (Gag) polyprotein – work together to confer drug resistance against protease inhibitors and compensate the mutations affecting viral fitness.
ReadAn Alternative HIV-1 Non-Nucleoside Reverse Transcriptase Inhibition Mechanism: Targeting the p51 Subunit
The ongoing development of drug resistance in HIV continues to push for the need of alternative drug targets in inhibiting HIV. One such target is the Reverse transcriptase (RT) enzyme which is unique and critical in the viral life cycle—a rational target that is likely to have less off-target effects in humans.
ReadConcentration- and pH-dependent oligomerization of the thrombin-derived C-terminal peptide TCP-25.
Keywords: oligomerization; thrombin; peptide self-assembly; antimicrobial peptide; pH- and/or concentration-sensitive oligomerization; TCP-25
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