Jacalin capped platinum nanoparticles confer persistent immunity against multiple Aeromonas infection in zebrafish

Abstract

Bacterial resistance is a major clinical problem, which is compounded by both a lack of new antibiotics and emergence of multi- and extremely-drug resistant microbes. In this context, non-toxic nanoparticles could play an important role in conferring protection against bacterial infections and in this study we have made an attempt to show the usefulness of jacalin capped platinum nanoparticles in protecting zebrafish against multiple infections with Aeromonas hydrophila. Our results also indicate that use of nanoparticles promotes adaptive immune response against the pathogen, so much so that zebrafish is able to survive repetitive infection even after twenty one days of being treated with jacalin-capped platinum nanoparticles. This is significant given that platinum salt is not antibacterial and jacalin is non-immunogenic. Our study for the first time reveals a novel mechanism of action of nanoparticles, which could form an alternate antibacterial strategy with minimal bacterial resistance.

Targeting the glycan of receptor binding domain with jacalin as a novel approach to develop a treatment against COVID-19

“…The change in the secondary structure of the model was analysed by DSSP approach [ 19 ]. The α-helical, β-strand and coil content of hACE2 was 62.41, 3.52 and 34.06, and RBD was 15.38, 24.10 and 60.51, respectively, which is consistent with the crystal structure [ 13 ]. The docking of jacalin–RBD complex with hACE2 affects the secondary structure content of RBD: α-helical (11.28), β-strand (26.15) and coil (62.56), whereas the secondary structure of hACE2 was not affected significantly, α-helical (60.90), β-strand (3.02) and coil (36.07).…”

“…The crystal structure of the novel corona spike RBD-ACE2 receptor (PDB ID: 6LZG) with 2.5 Å resolution was exploited in this work [13]. It consists of a concave RBD bound to claw-like structure on the surface of hACE2 (electronic supplementary material, figure S1).…”

“…Having learnt of the jacalin preference to RBD, we extend the analysis on the impact of the jacalin on RBD-hACE2 complex. It is noted from the crystal structure, the NAGs of hACE2 were not involved in RBD-hACEs interaction [13]. Thus, the NAGs of hACE2 were not considered for docking jacalin-RBD complex with hACE2.…”

“…In another study, we found that jacalin-PtNPs (JPtNPs) not only rescue zebrafish from bacterial infection but also protect it from re-infection after many days. The results showed that JPtNPs protect the animal from bacterial infection through modulating pro-inflammatory cytokines and promote bacteria-specific antibody response to sustain repetitive infection [13]. Pioneering work by Corbeau et al showed that jacalin binds to HIV-1 envelope glycoprotein (gp120) and its precursor (gp160) and inhibits the HIV-1 infection of CD4 + lymphoblastoid cells [11].…”

“…Recently, we found that jacalin recognizes the bacterial cell surface glycan and enhances the antimicrobial activity of nanoparticles [12]. Jacalin capped platinum nanoparticles exhibit excellent antimicrobial activity and promote adaptive immune response in a host to suppress repeated bacterial infection [13]. Hence, we hypothesize that jacalin can be considered to develop targeted therapies against COVID-19.…”