Background: Mostly BLIPs are identified in soil bacteria Streptomyces and originally isolated from
Streptomyces clavuligerus and can be utilized as a model system for biophysical, structural, mutagenic and computational
studies. BLIP possess homology with two proteins viz., BLIP-I (Streptomyces exofoliatus) and BLP
(beta-lactamase inhibitory protein like protein from S. clavuligerus). BLIP consists of 165 amino acid, possessing
two homologues domains comprising helix-loop-helix motif packed against four stranded beta-sheet resulting into
solvent exposed concave surface with extended four stranded beta-sheet. BLIP-I is a 157 amino acid long protein
obtained from S. exofoliatus having 37% sequence identity to BLIP and inhibits beta-lactamase.
Methods: This review is intended to briefly illustrate the beta-lactamase inhibitory activity of BLIP via proteinprotein
interaction and aims to open up a new avenue to combat antimicrobial resistance using peptide based
Results: D49A mutation in BLIP-I results in a decrease in affinity for TEM-1 from 0.5 nM to 10 nM (Ki). It is
capable of inhibiting TEM-1 and bactopenemase and differs from BLIP only in modulating cell wall synthesis
enzyme. Whereas, BLP is a 154 amino acid long protein isolated from S. clavuligerus via DNA sequencing
analysis of Cephamycin-Clavulanate gene bunch. It shares 32% sequence similarity with BLIP and 42% with
BLIP-I. Its biological function is unclear and lacks beta-lactamase inhibitory activity.
Conclusion: Protein-protein interactions mediate a significant role in regulation and modulation of cellular developments
and processes. Specific biological markers and geometric characteristics are manifested by active site
binding clefts of protein surfaces which determines the specificity and affinity for their targets. TEM1.BLIP is a
classical model to study protein-protein interaction. β-Lactamase inhibitory proteins (BLIPs) interacts and inhibits
various β-lactamases with extensive range of affinities.