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2007 ; 370
(4
): 701-13
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Structure of a complex of human lactoferrin N-lobe with pneumococcal surface
protein a provides insight into microbial defense mechanism
#MMPMID17543335
Senkovich O
; Cook WJ
; Mirza S
; Hollingshead SK
; Protasevich II
; Briles DE
; Chattopadhyay D
J Mol Biol
2007[Jul]; 370
(4
): 701-13
PMID17543335
show ga
Human lactoferrin, a component of the innate immune system, kills a wide variety
of microorganisms including the Gram positive bacteria Streptococcus pneumoniae.
Pneumococcal surface protein A (PspA) efficiently inhibits this bactericidal
action. The crystal structure of a complex of the lactoferrin-binding domain of
PspA with the N-lobe of human lactoferrin reveals direct and specific
interactions between the negatively charged surface of PspA helices and the
highly cationic lactoferricin moiety of lactoferrin. Binding of PspA blocks
surface accessibility of this bactericidal peptide preventing it from penetrating
the bacterial membrane. Results of site-directed mutagenesis, in vitro protein
binding assays and isothermal titration calorimetry measurements corroborate that
the specific electrostatic interactions observed in the crystal structure
represent major associations between PspA and lactoferrin. The structure provides
a snapshot of the protective mechanism utilized by pathogens against the host's
first line of defense. PspA represents a major virulence factor and a promising
vaccine candidate. Insights from the structure of the complex have implications
for designing therapeutic strategies for treatment and prevention of pneumococcal
diseases that remain a major public health problem worldwide.
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