Interaction of the HIV-1 gp120 viral protein V3 loop with bacterial lipopolysaccharide: a pattern recognition inhibition.

HIV-1 represents an elusive target for therapeutic compounds due to its high rate of mutation. Targeting structural patterns instead of a constantly changing specific three-dimensional structure may represent an approach that is less sensitive to viral mutations. The V3 loop of gp120 of HIV-1, which is responsible for binding of viral gp120 to CCR5 or CXCR4 coreceptors, has already been identified as an effective target for the inhibition of viral entry.

Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion.

Prion diseases are fatal transmissible neurodegenerative diseases affecting many mammalian species. The normal prion protein (PrP) converts into a pathological aggregated form, PrPSc, which is enriched in the β-sheet structure. Although the high resolution structure of the normal PrP was determined, the structure of the converted form of PrP remains inaccessible to high resolution techniques.

Essential roles of hydrophobic residues in both MD-2 and toll-like receptor 4 in activation by endotoxin.

Gram-negative bacterial endotoxin (i.e. lipopolysaccharide (LPS)) is one of the most potent stimulants of the innate immune system, recognized by the TLR4.

Taxanes inhibit human TLR4 signaling by binding to MD-2.

LPS is the primary ligand of Toll-like receptor 4, activating it through binding to its accessory protein MD-2. Murine but not human cells expressing MD-2/TLR4 are also activated by paclitaxel. Paclitaxel binds to human MD-2.

Structural aspects of peptides with immunomodulating activity.

The main function of the innate immune system from insects to mammals is to detect the presence of and act against invading microorganisms by recognizing their unique molecular signatures, most importantly, components of bacterial cell walls. A large number of peptides and derivatives, both synthetic and of natural origin, are known to influence immune responses in mammals by interacting with the conserved microbial structures, making the former attractive targets for drug development. This review focuses on structural aspects of the immunomodulating peptides and their receptors, including primary constitution, stereochemistry, conformation, binding and hydrophobic properties.