Enhancing the insecticidal potential of a baculovirus by overexpressing the mammalian ß-galactosyl binding protein galectin-1.

BACKGROUND: Bio-pesticide development is an important area of research in agriculture, in which viruses are an essential tool. Infection by entomological pathogenic viruses kills agricultural pests, and viral progenies are disseminated to infect more pests, eventually achieving long-term pest control in the field. Of the current virus-based pest control models, Autographa californica multiple nucleopolyhedrovirus (AcMNPV) is the most studied. AcMNPV belongs to the Baculoviridae family and can infect many lepidopterans. Although AcMNPV has been previously demonstrated to be a potential pest-control tool, its long virus infection cycle has made field applications challenging. To overcome this, we generated a recombinant baculovirus that can express mammalian galectin-1, which is a galactoside-binding protein that binds to the peritrophic matrix in the midgut of lepidopteran pests and induces perforation of the membrane. RESULTS: Hosts infected with a recombinant virus that expressed mammalian galectin-1 exhibited reduced appetite and died sooner in both laboratory and small-scale field studies, suggesting that the overexpression of galectin-1 can more efficiently eliminate pest hosts. In addition to disrupting the integrity of the peritrophic matrix, the immune system of hosts infected with recombinant baculovirus carrying the galectin-1 gene was suppressed, making hosts more vulnerable to secondary infection. CONCLUSION: Galectin-1 has been shown to affect immune responses in mammals, including humans, but to our knowledge, the effect of galectin-1 on insect immune systems had not been previously reported. Our results demonstrated that the pest-control potential of baculoviruses can be improved by using a recombinant baculovirus that overexpresses mammalian galectin-1 in hosts. © 2022 Society of Chemical Industry.

Candida albicans Sfp1 Is Involved in the Cell Wall and Endoplasmic Reticulum Stress Responses Induced by Human Antimicrobial Peptide LL-37.

Candida albicans is a commensal fungus of humans but can cause infections, particularly in immunocompromised individuals, ranging from superficial to life-threatening systemic infections. The cell wall is the outermost layer of C. albicans that interacts with the host environment. Moreover, antimicrobial peptides (AMPs) are important components in innate immunity and play crucial roles in host defense. Our previous studies showed that the human AMP LL-37 binds to the cell wall of C. albicans, alters the cell wall integrity (CWI) and affects cell adhesion of this pathogen. In this study, we aimed to further investigate the molecular mechanisms underlying the C. albicans response to LL-37. We found that LL-37 causes cell wall stress, activates unfolded protein response (UPR) signaling related to the endoplasmic reticulum (ER), induces ER-derived reactive oxygen species and affects protein secretion. Interestingly, the deletion of the SFP1 gene encoding a transcription factor reduced C. albicans susceptibility to LL-37, which is cell wall-associated. Moreover, in the presence of LL-37, deletion of SFP1 attenuated the UPR pathway, upregulated oxidative stress responsive (OSR) genes and affected bovine serum albumin (BSA) degradation by secreted proteases. Therefore, these findings suggested that Sfp1 positively regulates cell wall integrity and ER homeostasis upon treatment with LL-37 and shed light on pathogen-host interactions.