Target intelligence / Profile preview

Klebsiella pneumoniae cell-surface receptors (K. pneumoniae surface receptors)

Target
K. pneumoniae surface receptors
Molecular classification
Bacterial surface protein, Polysaccharide, Lipopolysaccharide, Outer membrane protein, Adhesin, Porin
01

Overview

Klebsiella pneumoniae cell-surface receptors comprise a diverse group of structural and functional molecules, including the capsular polysaccharide (CPS), lipopolysaccharide (LPS), outer membrane proteins (OMPs), and fimbriae. The CPS, or K-antigen, is the primary virulence factor, forming a thick layer that shields the bacterium from phagocytosis and complement-mediated killing. LPS, or O-antigen, serves as a major structural component and a potent endotoxin that triggers host inflammatory responses via Toll-like receptor 4 (TLR4). OMPs such as OmpK35 and OmpK36 function as porins for nutrient and antibiotic entry, while fimbriae like MrkA facilitate adhesion to host tissues and biofilm formation. These surface structures are critical therapeutic targets; they serve as the primary docking sites for bacteriophages and are the focus of monoclonal antibody and vaccine development aimed at treating multidrug-resistant (MDR) and hypervirulent (hvKp) strains. Targeting these receptors is essential for overcoming the high mortality rates associated with carbapenem-resistant Klebsiella pneumoniae (CRKP) infections.

Other names
Klebsiella pneumoniae surface antigensK. pneumoniae cell wall componentsK. pneumoniae phage receptorsK. pneumoniae surface proteinsK. pneumoniae virulence factors
02

Mechanism of action

Drugs and biologicals targeting these receptors work through several mechanisms: polymyxins bind to lipopolysaccharides (LPS) to disrupt outer membrane integrity; monoclonal antibodies bind to capsular polysaccharides (CPS) or O-antigens to promote opsonophagocytic killing by host neutrophils; bacteriophages utilize these surface structures as entry receptors to initiate lytic infection; and siderophore-conjugated antibiotics like cefiderocol exploit iron-uptake receptors to bypass porin-mediated resistance.

03

Biological functions

AdhesionBiofilm formationImmune evasionNutrient acquisitionVirulence factorMembrane permeability
04

Disease associations

InfectionPneumoniaSepsisUrinary tract infectionMeningitisLiver abscess
05

Safety considerations

Endotoxin-mediated systemic inflammation (Jarisch-Herxheimer-like reaction)Emergence of phage resistance through receptor mutationSerotype replacement or switching in response to vaccinesReduced drug permeability due to porin loss or modification
06

Interacting drugs

Polymyxin B

6 more in the full profile.

07

Biomarkers

K-antigen serotype (e.g., K1, K2)O-antigen serotype (e.g., O1, O2)OmpK36 expression levelHypermucoviscosity phenotype

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