Tuberculosis/COVID-19 co-infection detected in a single sputum sample using a rapid molecular test.

Tuberculosis (TB) and COVID-19 affect the lungs and are transmitted mainly by aerosols or particles of saliva from infected persons. Clinical similarities between diseases can affect correct diagnosis. Individuals belonging to the population deprived of liberty (PDL) are at increased risk of contagion due to precarious sanitary conditions and overcrowded environments. A variety of specimens may be suitable for the diagnosis of COVID-19, using molecular diagnostic techniques; however, there is little data on the analysis of sputum samples with the Xpert Xpress SARS-CoV-2® for the diagnosis of COVID-19, especially in this population group. The present study reports a case of TB and COVID-19 co-infection detected in sputum from an individual belonging to the PDL. For the detection, it used the GeneXpert platform (Cepheid, USA). Mycobacterium tuberculosis complex (MTC) was detected using the Xpert MTB/RIF Ultra® cartridge and SARS-CoV-2 was detected using the Xpert Xpress SARS-CoV-2® cartridge. The genes IS6110 and IS1081 were detected within 80 min indicating the presence of MTC, with no mutations related to resistance to rifampicin. The SARS-CoV-2 E and N2 genes were detected within 45 min. The result was confirmed by RT-qPCR with detection of E, N, and RdRP/S genes in the sputum and nasopharyngeal (NP) specimens. Rapid diagnoses that allow the identification and differentiation of such diseases are important for adequate epidemiological surveillance, isolation of infected individuals, and interruption of the transmission chain. Using the GeneXpert platform, specimens can be tested as soon as they are received, without the need for prior preparation. The US Food and Drug Administration has issued emergency authorization for the use of the Cepheid Xpert Xpress SARS-CoV-2 for the rapid detection of SARS-CoV-2 using specimens from a NP or nasal wash/aspirate. The case presented here gains an innovation with the use of the sputum to COVID-19 diagnosis.

Encrypted antimicrobial peptides from proteins present in the plasma of the millipede Rhinocricus sp.

Millipedes are among the most diverse and abundant arthropods in terrestrial environments. However, little is known about their innate immune response against invading pathogenic microorganisms, which is very intriguing considering that the evolutionary success of millipedes is largely due to this complex and primitive defense system, since it allowed them to colonize a wide variety of microhabitats characterized by their high microbial proliferation. Accordingly, the aim of the present work was to determine the presence of antimicrobial peptides in the hemolymph of the millipede Rhinocricus sp. in total, four native peptides with potent antimicrobial activity against different microorganisms, lack of cytotoxicity against Vero cells and lack of hemolytic effects against human erythrocytes were isolated and named RP40–16, RP40–19, RP40–20/1 and RP40–20/2. The analysis with bioinformatics tools suggested that these peptides may be encrypted in large proteins present in the plasma: Hemocyanin and thioester-containing protein. Considering these results, it can be said that millipede hemolymph represents a promising source of molecules with potential for the development of non-conventional antibiotics. Therefore, in order to have a clearer notion of the biotechnological potential and the role of these peptides in the innate immune response of Rhinocricus sp., future studies should focus on elucidating their mechanisms of action, as well as additional biological properties

Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes

One of the most important cellular events in arthropods is the moulting of the cuticle (ecdysis). This process allows them to grow until they reach sexual maturity. Nevertheless, during this stage, the animals are highly exposed to pathogens. Consequently, it can be assumed that arthropods counter with an efficient anti-infective strategy that facilitates their survival during ecdysis. Herein, we characterized a novel antimicrobial peptide called Pinipesin, present in the exuviae extract of the centipede Scolopendra subspinipes subspinipes. The antimicrobial activity of Pinipesin was tested. The haemolytic activity of the peptide was evaluated and its possible mechanism of action was investigated. Identification was carried out by mass spectrometry analysis. Pinipesin displayed potent antimicrobial effects against different microorganisms and showed low haemolytic effects against human erythrocytes at high concentrations. It has a monoisotopic mass of 1213.57 Da, its sequence exhibited high similarity with some cuticular proteins, and it might act intracellularly by interfering with protein synthesis. Our data suggest that Pinipesin might be part of a prophylactic immune response during the ecdysis process of centipedes. Therefore, it is a promising candidate for the development of non-conventional antibiotics that could help fight infectious diseases and represents an exciting discovery for this taxon.

Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes

One of the most important cellular events in arthropods is the moulting of the cuticle (ecdysis). This process allows them to grow until they reach sexual maturity. Nevertheless, during this stage, the animals are highly exposed to pathogens. Consequently, it can be assumed that arthropods counter with an efficient anti-infective strategy that facilitates their survival during ecdysis. Herein, we characterized a novel antimicrobial peptide called Pinipesin, present in the exuviae extract of the centipede Scolopendra subspinipes subspinipes. The antimicrobial activity of Pinipesin was tested. The haemolytic activity of the peptide was evaluated and its possible mechanism of action was investigated. Identification was carried out by mass spectrometry analysis. Pinipesin displayed potent antimicrobial effects against different microorganisms and showed low haemolytic effects against human erythrocytes at high concentrations. It has a monoisotopic mass of 1213.57 Da, its sequence exhibited high similarity with some cuticular proteins, and it might act intracellularly by interfering with protein synthesis. Our data suggest that Pinipesin might be part of a prophylactic immune response during the ecdysis process of centipedes. Therefore, it is a promising candidate for the development of non-conventional antibiotics that could help fight infectious diseases and represents an exciting discovery for this taxon.

Loxosceles gaucho spider venom: an untapped source of antimicrobial agents

The remarkable ability of microorganisms to develop resistance to conventional antibiotics is one of the biggest challenges that the pharmaceutical industry currently faces. Recent studies suggest that antimicrobial peptides discovered in spider venoms may be useful resources for the design of structurally new anti-infective agents effective against drug-resistant microorganisms. In this work, we found an anionic antibacterial peptide named U-1-SCRTX-Lg1a in the venom of the spider Loxosceles gaucho. The peptide was purified using high-performance liquid chromatography (HPLC), its antimicrobial activity was tested through liquid growth inhibition assays, and its chemical properties were characterized using mass spectrometry. U-1-SCRTX-Lg1a was found to show a monoisotopic mass of 1695.75 Da, activity against Gram-negative bacteria, a lack of hemolytic effects against human red blood cells, and a lack of cytotoxicity against human cervical carcinoma cells (HeLa). Besides this, the sequence of the peptide exhibited great similarity to specific regions of phospholipases D from different species of Loxosceles spiders, leading to the hypothesis that U-1-SCRTX-Lg1a may have originated from a limited proteolytic cleavage. Our data suggest that U-1-SCRTX-Lg1a is a promising candidate for the development of new antibiotics that could help fight bacterial infections and represents an exciting discovery for Loxosceles spiders.

Loxosceles gaucho spider venom: an untapped source of antimicrobial agents

The remarkable ability of microorganisms to develop resistance to conventional antibiotics is one of the biggest challenges that the pharmaceutical industry currently faces. Recent studies suggest that antimicrobial peptides discovered in spider venoms may be useful resources for the design of structurally new anti-infective agents effective against drug-resistant microorganisms. In this work, we found an anionic antibacterial peptide named U-1-SCRTX-Lg1a in the venom of the spider Loxosceles gaucho. The peptide was purified using high-performance liquid chromatography (HPLC), its antimicrobial activity was tested through liquid growth inhibition assays, and its chemical properties were characterized using mass spectrometry. U-1-SCRTX-Lg1a was found to show a monoisotopic mass of 1695.75 Da, activity against Gram-negative bacteria, a lack of hemolytic effects against human red blood cells, and a lack of cytotoxicity against human cervical carcinoma cells (HeLa). Besides this, the sequence of the peptide exhibited great similarity to specific regions of phospholipases D from different species of Loxosceles spiders, leading to the hypothesis that U-1-SCRTX-Lg1a may have originated from a limited proteolytic cleavage. Our data suggest that U-1-SCRTX-Lg1a is a promising candidate for the development of new antibiotics that could help fight bacterial infections and represents an exciting discovery for Loxosceles spiders.