Rational Design of an Antimicrobial Peptide Based on Structural Insight into the Interaction of Pseudomonas aeruginosa Initiation Factor 1 with Its Cognate 30S Ribosomal Subunit

2021 ◽  
Author(s):  
Nicolette Valdez ◽  
Casey Hughes ◽  
Stephanie O. Palmer ◽  
Alyssa Sepulveda ◽  
Frank B. Dean ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antimicrobial Peptide ◽  
Rational Design ◽  
Ribosomal Subunit ◽  
Initiation Factor ◽  
Structural Insight ◽  
Insight Into

Structural Insight into Multivalent Galactoside Binding to Pseudomonas aeruginosa Lectin LecA

2015 ◽  
Vol 10 (11) ◽  
pp. 2455-2462 ◽  
Author(s):  
Ricardo Visini ◽  
Xian Jin ◽  
Myriam Bergmann ◽  
Gaelle Michaud ◽  
Francesca Pertici ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Structural Insight ◽  
Insight Into

scholarly journals Structural Insight into the Antibiotic Action of Telithromycin against Resistant Mutants

2003 ◽  
Vol 185 (14) ◽  
pp. 4276-4279 ◽  
Author(s):  
Rita Berisio ◽  
Joerg Harms ◽  
Frank Schluenzen ◽  
Raz Zarivach ◽  
Harly A. S. Hansen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Deinococcus Radiodurans ◽  
Ribosomal Subunit ◽  
Large Ribosomal Subunit ◽  
Resistant Strains ◽  
Structural Insight ◽  
Resistant Mutants ◽  
Exit Tunnel ◽  
Structural Insights ◽  
Insight Into

ABSTRACT The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.

scholarly journals Structural insight into the dual function of LbpB in mediating Neisserial pathogenesis

2021 ◽  
Author(s):  
Nicholas Noinaj ◽  
Ravi Yadav ◽  
Srinivas Govindan ◽  
Courtney Daczkowski ◽  
Andrew Mesecar ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Iron Acquisition ◽  
Bound State ◽  
Dual Function ◽  
Membrane Transporter ◽  
Binding Studies ◽  
Cationic Antimicrobial Peptide ◽  
Structural Insight ◽  
Insight Into ◽  
Dual Functions

Lactoferrin binding protein B (LbpB) is a lipoprotein present on the surface of Neisseria that has been postulated to serve dual functions during pathogenesis in both iron acquisition from lactoferrin, and in providing protection against the cationic antimicrobial peptide lactoferricin. Here, we present the structures of LbpB from N. meningitidis and N. gonorrhoeae in complex with human holo-lactoferrin, forming a 1:1 complex and confirmed by SEC-SAXS. LbpB consists of N- and C-lobes with the N-lobe interacting extensively with the C-lobe of lactoferrin. Our structures provides insight into LbpB's preference towards holo-lactoferrin, and our mutagenesis and binding studies show that lactoferrin and lactoferricin bind independently. Our studies provide the molecular details for how LbpB serves to capture and preserve lactoferrin in an iron-bound state for delivery to the membrane transporter LbpA for iron piracy, and as an antimicrobial peptide sink to evade host immune defenses.

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