Antimicrobial peptides from<i>Bombyx mori</i>: a splendid immune defense response in silkworms

Nesa, Jannatun; Sadat, Abdul; Buccini, Danieli Fernanda; Katı, Ahmet; Mandal, Amit Kumar; Franco, Octávio L.

doi:10.1039/c9ra06864c

Cited by 50 publications

(35 citation statements)

References 92 publications

(171 reference statements)

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“…Insects oils are rich in other putative antimicrobials such as antimicrobial peptides (AMP), polymers, and chemical complexes that could act alone or synergically with fatty acids [ 34 , 35 , 52 , 53 ]. A recent “in silico” transcriptomic analysis of H. illucens brought to the identification of 57 peptides with putative antimicrobial activity and belonging to cecropin and defensin families [ 54 ]; on the other hand, six families of AMP have been identified in B. mori , namely cecropin, defensin, moricin, gloverin, attacin, and lebocin [ 55 ].…”

Section: Discussionmentioning

confidence: 99%

Mechanical Processing of Hermetia illucens Larvae and Bombyx mori Pupae Produces Oils with Antimicrobial Activity

Saviane

Tassoni

Lupi

et al. 2021

Animals

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The aim of this work was to develop processing methods that safeguard the quality and antimicrobial properties of H. illucens and B. mori oils. We adopted a vegetable diet for both insects: leftover vegetables and fruit for H. illucens and mulberry leaves for B. mori. First, alternative techniques to obtain a good oil extraction yield from the dried biomass of H. illucens larvae were tested. Traditional pressing resulted to be the best system to maximize the oil yield and it was successfully applied to B. mori pupae. Oil quality resulted comparable to that obtained with other extraction methods described in the literature. In the case of B. mori pupae, different treatments and preservation periods were investigated to evaluate their influence on the oil composition and quality. Interestingly, agar diffusion assays demonstrated the sensitivity of Gram-positive Bacillus subtilis and Staphylococcus aureus to H. illucens and B. mori derived oils, whereas the growth of Gram-negative Pseudomonas aeruginosa and Escherichia coli was not affected. This study confirms that fat and other active compounds of the oil extracted by hot pressing could represent effective antimicrobials against bacteria, a relevant result if we consider that they are by-products of the protein extraction process in the feed industry.

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Section: Discussionmentioning

confidence: 99%

Mechanical Processing of Hermetia illucens Larvae and Bombyx mori Pupae Produces Oils with Antimicrobial Activity

Saviane

Tassoni

Lupi

et al. 2021

Animals

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“…AMP study is based on the discovery of the antimicrobial activity of peptides in fluids and tissues of humans and mammals [ 31 ]. Subsequent studies showed that AMPs play an important role in the immune system of all living beings [ 32 ]. The development of physicochemical methods for studying molecular processes made it possible to describe the structural features of peptides and to reveal some connections between the properties of AMPs.…”

Section: Brief History Of Research Physicochemical Properties CLmentioning

confidence: 99%

Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?

Kurpe

Grishin

Surin

et al. 2020

IJMS

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At present, much attention is paid to the use of antimicrobial peptides (AMPs) of natural and artificial origin to combat pathogens. AMPs have several points that determine their biological activity. We analyzed the structural properties of AMPs, as well as described their mechanism of action and impact on pathogenic bacteria and viruses. Recently published data on the development of new AMP drugs based on a combination of molecular design and genetic engineering approaches are presented. In this article, we have focused on information on the amyloidogenic properties of AMP. This review examines AMP development strategies from the perspective of the current high prevalence of antibiotic-resistant bacteria, and the potential prospects and challenges of using AMPs against infection caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).

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“…Former studies about AMP antimicrobial activity against B. thuringiensis showed that AMP encoding genes from Trichoplusia ni were increased in insects which were previously exposed to these bacteria [ 63 ]. Also, cecropins, moricins and gloverins from Bombyx mori showed a high antimicrobial activity against B. thuringiensis [ 64 ]. In Spodoptera spp, the response to B. thuringiensis infection depends on several biological factors, such as the production of AMPs [ 65 ].…”

Section: Discussionmentioning

confidence: 99%

“…When this barrier is broken, invading microorganisms are exposed to a variety of cellular and humoral processes that support the host defense [ 4 ]. In that regard, the production of antimicrobial peptides (AMPs) is one of the key responses in the humoral immune system [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and recombinant expression of an antimicrobial peptide (cecropin B-like) from soybean pest Anticarsia gemmatalis

Ramos¹,

Rangel²,

Andrade³

et al. 2021

J. Venom. Anim. Toxins incl. Trop. Dis

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Background Insects can be found in numerous diverse environments, being exposed to pathogenic organisms like fungi and bacteria. Once these pathogens cross insect physical barriers, the innate immune system operates through cellular and humoral responses. Antimicrobial peptides are small molecules produced by immune signaling cascades that develop an important and generalist role in insect defenses against a variety of microorganisms. In the present work, a cecropin B-like peptide (AgCecropB) sequence was identified in the velvetbean caterpillar Anticarsia gemmatalis and cloned in a bacterial plasmid vector for further heterologous expression and antimicrobial tests. Methods AgCecropB sequence (without the signal peptide) was cloned in the plasmid vector pET-M30-MBP and expressed in the Escherichia coli BL21(DE3) expression host. Expression was induced with IPTG and a recombinant peptide was purified using two affinity chromatography steps with Histrap column. The purified peptide was submitted to high-resolution mass spectrometry (HRMS) and structural analyses. Antimicrobial tests were performed using gram-positive ( Bacillus thuringiensis ) and gram-negative ( Burkholderia kururiensis and E. coli ) bacteria. Results AgCecropB was expressed in E. coli BL21 (DE3) at 28°C with IPTG 0.5 mM. The recombinant peptide was purified and enriched after purification steps. HRMS confirmed AgCrecropB molecular mass (4.6 kDa) and circular dichroism assay showed α-helix structure in the presence of SDS. AgCrecropB inhibited almost 50% of gram-positive B. thuringiensis bacteria growth. Conclusions The first cecropin B-like peptide was described in A. gemmatalis and a recombinant peptide was expressed using a bacterial platform. Data confirmed tertiary structure as predicted for the cecropin peptide family. AgCecropB was capable to inhibit B. thuringiensis growth in vitro .

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Antimicrobial peptides fromBombyx mori: a splendid immune defense response in silkworms

Abstract: AMPs produced by B. mori induced by microbial challenge in the fat body.

Cited by 50 publications

References 92 publications

Mechanical Processing of Hermetia illucens Larvae and Bombyx mori Pupae Produces Oils with Antimicrobial Activity

Mechanical Processing of Hermetia illucens Larvae and Bombyx mori Pupae Produces Oils with Antimicrobial Activity

Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?

Identification and recombinant expression of an antimicrobial peptide (cecropin B-like) from soybean pest Anticarsia gemmatalis

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