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Biapenem, Ritipenem, Panipenem, and Sulopenem
Published in 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, 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
Published in Dongyou Liu, 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
A 2018–2019 patent review of metallo beta-lactamase inhibitors
Published in Expert Opinion on Therapeutic Patents, 2020
Nakita Reddy, Mbongeni Shungube, Per I Arvidsson, Sooraj Baijnath, Hendrik G Kruger, Thavendran Govender, Tricia Naicker
CRE’s producing metallo beta-lactamases are clinically catastrophic and are often termed as ‘nightmare bacteria’ [20], due to treatment difficulty and wide dissemination [17]. These MBLs include the New Delhi MBL (NDM) [21], Verona Integrase MBL (VIM) [22], and Imipenemase MBL (IMP) [15,23], all belonging to the B1 subclass. Therefore, subclass B1 is of clinical importance and contains the largest number of members [18]. Subclass B2 contains the least number of members and includes producers such as, Serratia fonticola Sfh-I [24], Aeromonas sobria ImiS [25], and Aeromonas hydrophila CphA [26]. Whilst, Chryseobacterium meningosepticum GOB-1 [27] and Stenotrophomonas (Xanthomonas) maltophilia L1 [28] are members of subclass B3.
Toxicological and behavioral study of two potential antibacterial agents:4-chloromercuribenzoic acid and quercetin on Swiss-albino mice
Published in Drug and Chemical Toxicology, 2020
Till date, several high throughput screening (HTS) studies of pharmacologically active and click chemistry compound libraries have identified 4-chloromercuribenzoic acid (pCMB) as a candidate carbapenemase inhibitor (Minond et al. 2009, Thomas et al. 2013). In presence of dicloxacillin, pCMB can irreversibly inhibit beta-lactamase-I activity from Bacillus cereus (Amicosante et al. 1987). Moreover, pCMB exhibited selective advantage over commercially available beta-lactamase inhibitors in inhibiting carbapenem hydrolysis by AsbM1, purified from Aeromonas sobria (Yang and Bush 1996). It was also found to potentiate imipenem efficacy and demonstrated synergy with imipenem against transformed Escherichia coli BL21/VIM-2 (Minond et al. 2009). On the other hand, quercetin, a flavonol abundantly found in several plant foods such as onions/shallots, citrus fruits/berries, cruciferous vegetables, and tea, has long been known for its antioxidant, antiviral, anticancer, antimicrobial, and anti-inflammatory activities (Maalik et al. 2014, Li et al. 2016). Hence, it could be a promising candidate for the treatment of CR-GNB mediated infections. Some recent studies predicted that presence of quercetin in Berberis aristata and Camellia sinensis extracts, which could ameliorate efficacy of third line antibiotics against carbapenem resistant beta-lactamase producing E. coli (Thakur et al. 2016a, 2016b). Moreover, quercetin exhibited synergism with amoxicillin and ceftazidime against Staphylococcus epidermidis and Streptococcus pyrogens, respectively (Siriwong et al. 2015, 2016).