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AlphaFold reveals how pathogenic Leptospira use cross-kingdom thiol-disulfide exchange to evade the complement membrane attack complex
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AlphaFold reveals how pathogenic Leptospira use cross-kingdom thiol-disulfide exchange to evade the complement membrane attack complex
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Journal Article
AlphaFold reveals how pathogenic Leptospira use cross-kingdom thiol-disulfide exchange to evade the complement membrane attack complex
2026
Overview
Leptospirosis is a globally important zoonotic disease of humans and animals, caused by the bacteria Leptospira. A central determinant of virulence is the ability for these bacteria to evade complement, a host defense system that assembles the membrane attack complex to eliminate pathogens. Here, we elucidate a novel immune evasion mechanism in which the leptospiral surface protein LIC13259 forms a disulfide bond with complement component C8γ, preventing binding of C8α. This interaction disrupts the membrane attack complex assembly and promotes bacterial survival. To our knowledge, this represents the first example of a cross-kingdom disulfide bond mediating bacterial pathogenesis. These findings provide novel insights into leptospiral immune modulation and demonstrate the power of AlphaFold-based structural predictions to reveal unique host-pathogen interactions.
Publisher
ASM,American Society for Microbiology (ASM),American Society for Microbiology
Subject
/ Animals
/ Bacterial Complement Inhibitors
/ Bacterial Complement Resistance
/ Clinical Microbiology and Infectious Diseases
/ Complement in Pathogen Evasion
/ Complement Membrane Attack Complex - immunology
/ Complement Membrane Attack Complex - metabolism
/ Humans
/ Leptospirosis - microbiology
/ membrane attack complex (MAC)
/ Microbial Pathogenesis and Immunology
/ Microbial Physiology and Genetics
/ Sulfhydryl Compounds - chemistry
