Biapenem, Ritipenem, Panipenem, and Sulopenem
M. Lindsay Grayson, Sara E. Cosgrove, Suzanne M. Crowe, M. Lindsay Grayson, William Hope, James S. McCarthy, John Mills, Johan W. Mouton, David L. Paterson in Kucers’ The Use of Antibiotics, 2017
Biapenem is effective against most strains of Moraxella catarrhalis, Aeromonas hydrophila, and Acinetobacter spp. (Yoshida et al., 2006; Suzuki et al., 2001; Hoban et al., 1993). When a higher inoculum (106 colony forming units [CFUs]) of A. hydrophila and Aeromonas sobria was used, MIC90 of biapenem increased 32-fold compared with when the standard 104 colony forming units were inoculated (Clarke and Zemcov, 1993). With Acinetobacter spp., the MIC50 of biapenem against 250 imipenem-resistant strains isolated from a Spanish hospital between 1991 and 1996 was 4- and 8-fold lower than those of imipenem and meropenem, respectively. However, MICs were always above 32 µg/ml (Ruiz et al., 1999). Burkholderia pseudomallei is susceptible to biapenem (Smith et al., 1996), but MIC50 and MIC90 for Burkholderia cepacia is higher than those for B. pseudomallei. In particular, strains isolated from cystic fibrosis patients tended to have high MICs (Pitt et al., 1996). Stenotrophomonas maltophilia is resistant to biapenem (Hoban et al., 1993).
Aeromonas
Dongyou Liu in Handbook of Foodborne Diseases, 2018
Aeromonas species are gram-negative, oxidase-positive, facultative anaerobic rod-shaped bacteria in the family Aeromonadaceae that are ubiquitously distributed in aquatic environments and established pathogens of fish and marine animals.1 They are also associated with a wide spectrum of diseases in humans, including gastroenteritis, septicemia, skin and soft-tissue infections, biliary tract infection, and other uncommon infections.1 Human infections, predominated by gastroenteritis of either acute, self-limited diarrhea, or cholera-like illness, are increasingly recognized and reported, and their clinical variety is expanding. Although the involvement of aeromonads as enteropathogens has been questioned, their pathogenic role in causing human gastrointestinal infection is supported by accumulating evidence.1–3 Not only could aeromonads be isolated from different foods, but they could also be detected in returning travelers suffering from diarrhea. Globally three major species isolated from clinical, food, and water sources are Aeromonas hydrophila, Aeromonas veronii biovar sobria, and Aeromonas caviae. However, the list of newly identified Aeromonas species becomes longer and longer. In light of the rapidly evolving landscape around Aeromonas species, we present an overview on the clinical epidemiology, variation, and antimicrobial treatment of Aeromonas-induced gastroenteritis, the isolation of aeromonads from feces, and the putative virulence factors in aeromonads causing gastroenteritis, along with current evidence supporting the pathogenic role of aeromonads in human gastrointestinal infections.
Aeromonas
Dongyou Liu in Laboratory Models for Foodborne Infections, 2017
Currently, about 30 species are recognized in the genus Aeromonas, including Aeromonas aquatica, Aeromonas australiensis, Aeromonas bestiarum (HG2, formerly Aeromonas hydrophila genomospecies 2), Aeromonas bivalvium, Aeromonas cavernicola, Aeromonas caviae (HG4, synonym Aeromonas punctata), Aeromonas dhakensis (synonyms Aeromonas aquariorum, Aeromonas hydrophila subsp. dhakensis), Aeromonas diversa (HG13, synonym Aeromonas group 501), Aeromonas encheleia (HG16), Aeromonas eucrenophila (HG6), Aeromonas finlandensis, Aeromonas fluvialis, Aeromonas hydrophila (HG1, synonyms Bacillus hydrophilus fuscus, Bacillus hydrophilus, Proteus hydrophilus, Bacterium hydrophilum, Pseudomonas hydrophila), Aeromonas jandaei (HG9), Aeromonas lacus, Aeromonas media (HG5A, HG5B), Aeromonas molluscorum, Aeromonas piscicola, Aeromonas popoffii (HG17), Aeromonas rivuli, Aeromonas salmonicida (HG3), Aeromonas sanarellii, Aeromonas schubertii (HG12), Aeromonas simiae, Aeromonas sobria (HG7), Aeromonas taiwanensis, Aeromonas tecta, Aeromonas trota (HG14, synonym Aeromonas enteropelogenes), and Aeromonas veronii (HG8, HG10, synonyms Aeromonas ichthiosmia, Aeromonas allosaccharophila, Aeromonas culicicola) [1–3]. Interestingly, Aeromonas sharmana (which unlike other members of the genus, is negative for nitrate reductase, lysine or ornithine decarboxylase or arginine dihydrolase, and lacks deoxyribonuclease activity) is now considered to be non-Aeromonas although it may still fall within the family Aeromonadaceae [1].
Epithelial integrity, junctional complexes, and biomarkers associated with intestinal functions
Published in Tissue Barriers, 2022
Arash Alizadeh, Peyman Akbari, Johan Garssen, Johanna Fink-Gremmels, Saskia Braber
The PDZ and proline-rich domains of afadin have been associated with either direct or indirect interaction of afadin with different cell adhesion proteins, including nectin, E-cadherin, JAM-A, ZOs and CLDNs (Figure 4).64,75,112,116–118 It is already known that afadin plays a crucial role in establishment and proper organization of the apical junctional complexes as well as providing a physical link between different components of apical junctional complexes and the intracellular cytoskeleton.112,113,119 It has been reported that the architecture of epithelial apical junctions in both the small and large intestines are preserved in afadin-knockout mice; however, this lack of afadin results in impaired intestinal homeostasis and increased intestinal permeability.115 A study with T84 intestinal epithelial cells demonstrated that the consequence of Aeromonas sobria proteases induced decomposition in nection-2 and afadin leading to as alterations in intestinal barrier function.120Aeromonas species are known to cause human gastrointestinal infections.121 In addition, it is believed that afadin has a crucial role in recruitment of different TJ proteins to the apical side of the cell–cell adherens junctions, since afadin-depleted MDCK cells show a significant delay in the reassembly of TJs and it subsequently enhances epithelial permeability.64,116,117,122,123
Resistance trends and epidemiology of Aeromonas and Plesiomonas infections (RETEPAPI): a 10-year retrospective survey
Published in Infectious Diseases, 2019
A total of 193 individual isolates were identified (n = 193; 19.3 ± 12.3/year, highest in 2015 and lowest in 2010) from various sample types during the 10-year study period. The number of isolates between 2008 and 2012 was n = 46 (9.2 ± 4.2/year, range: 5–16) while for 2013–2017, this number was n = 147 (29.4 ± 8.2/year, range: 18–38); the difference in the isolation frequency was statistically significant (p = .0012). 51.8% of isolates originated from inpatient departments (p > .05). 75.6% of isolates were identified in the period between May and September of the relevant year. Most of the isolates were Aeromonas spp. (97.9%; namely: Aeromonas hydrophila 45.6%, Aeromonas caviae 36.7%, Aeromonas veronii 13.2%, Aeromonas salmonicida 3.3%, Aeromonas bestiarum 1.1% and Aeromonas ichtiosima 1.1%), while Plesiomonas shigelloides isolates were fewer (2.1%, one isolate in 2008, 2012, 2014 and 2016, respectively). Before 2013, A. hydrophila and A. caviae were mainly isolated.
Antimicrobial peptides (AMPs): a patent review (2015–2020)
Published in Expert Opinion on Therapeutic Patents, 2020
Giannamaria Annunziato, Gabriele Costantino
In 2017, Sanil et al. at the Indiana University Research and Technology Corporation Records [51], identified and selected for further studies two novel peptides belonging to brevinine-1 family (brevinine-1 HYba1 and brevinine-1 HYba2). Net charge and grand average of hydropathicity (GRAVY) of the peptides were computed using ProtPAram [52]. Peptide Synthetics were used to calculate the theoretical molecular mass of the peptides. Both brevinine-1 HYba1 (B1/1) and brevinin-1 HYba2 (B1/2) were synthesized in 3 forms, with C-terminal acid (B1/1 COOH and B1/2 COOH), C-terminal amide (B1/1 CONH2 and B1/2 CONH2) and cyclic peptide (cyclic B1/1 CONH2 and cyclic B1/2 CONH2) (Table 14). The peptides were synthesized through solid phase peptide synthesis technique (SPPS). Following deprotection and cleavage from the resin, the peptides were purified by reverse-phase HPLC. The purity of the final products was checked by MALDI-TOF MS. Broth dilution method was used to assess the antimicrobial activity of the peptides. Bacterial strains used for in vitro antibacterial assay were S. aureus (MTCC9542), Bacillus subtilis (MTCC14416), Bacillus coagulans (ATCC7050), MRSA (ATCC43300), S. mutans (MTCC497), S. gordonii (MTCC2695), Vibrio cholerae (MCV09), E. coli (ATCC25922), Vancomycin Resistant Enterococci (VRE) (ATCC29212) and Gram-negative fish pathogens Aeromonas hydrophila (ATCC7966) and Aeromonas sobria (ATCC43979) (Table 15). Hemolytic assay was carried out, too, showing a good safety profile of the peptides.
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