Isolation and characterization of an antimicrobial peptide from bovine hemoglobin α-subunit

Hu, Jianhe; Xu, Ming; Hang, Bolin; Wang, Lan; Wang, Qing; Chen, Junjie; Song, Tao; Fu, Dengfeng; Wang, Ziliang; Wang, Sanhu; Liu, Xingyou

doi:10.1007/s11274-010-0514-4

Cited by 48 publications

(27 citation statements)

References 13 publications

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“…P3 is an 18-residue peptide with modest antimicrobial activity and weak hemolytic activity (15). A series of analogs were created by substituting or removing specific amino acids in efforts to enhance P3 antimicrobial activity.…”

Section: Sequence Characteristicsmentioning

confidence: 99%

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Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model

Zhang

Wang

et al. 2015

Antimicrob Agents Chemother

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With the emergence of many antibiotic-resistant strains worldwide, antimicrobial peptides (AMPs) are being evaluated as promising alternatives to conventional antibiotics. P3, a novel hemoglobin peptide derived from bovine erythrocytes, exhibited modest antimicrobial activity in vitro. We evaluated the antimicrobial activities of P3 and an analog, JH-3, both in vitro and in vivo. The MICs of P3 and JH-3 ranged from 3.125 g/ml to 50 g/ml when a wide spectrum of bacteria was tested, including multidrug-resistant strains. P3 killed bacteria within 30 min by disrupting the bacterial cytoplasmic membrane and disturbing the intracellular calcium balance. Circular dichroism (CD) spectrometry showed that P3 assumed an ␣-helical conformation in bacterial lipid membranes, which was indispensable for antimicrobial activity. Importantly, the 50% lethal dose (LD 50 ) of JH-3 was 180 mg/kg of mouse body weight after intraperitoneal (i.p.) injection, and no death was observed at any dose up to 240 mg/kg body weight following subcutaneous (s.c.) injection. Furthermore, JH-3 significantly decreased the bacterial count and rescued infected mice in a model of mouse bacteremia. In conclusion, P3 and an analog exhibited potent antimicrobial activities and relatively low toxicities in a mouse model, indicating that they may be useful for treating infections caused by drug-resistant bacteria.T he overuse of traditional antibiotics has triggered the frequent emergence of multidrug-resistant (MDR) bacteria, which pose significant threats to public health. Bacterial resistance is usually attributable to mutations and can spread, rendering the problem worse (1-3). Extensively mutated bacteria become resistant to many conventional chemotherapeutics. Since the early 1960s, many novel antibiotics have been prepared, but these are usually chemical variations of older and conventional antibiotics (4). There is an urgent need to find novel antimicrobial agents that control infections caused by MDR bacteria.Antimicrobial peptides (AMPs) have recently attracted significant attention (5). They are primitive components of innate immune systems and play multiple roles in immune defense (6, 7). AMPs are widespread in unicellular organisms, plants, and animals, and more than 1,600 have been identified in a wide range of organisms (8-10). Most natural AMPs exhibit broad-spectrum activities against bacteria (including MDR bacteria), fungi, viruses (including HIV), and tumors (11-13). Although many potent AMPs have been identified, a lack of knowledge about the mechanisms of action and high-level AMP toxicities are major obstacles on the path to clinical use (14). Therefore, the design of novel potent AMPs exhibiting low toxicities in vivo and the identification of the mechanisms of AMP-membrane interactions are important for the development of novel antimicrobial agents.Recently, we reported the first isolation of P3, a component of the bovine hemoglobin ␣-subunit (15). Its primary sequence is VNFKLLSHSLLVTLASHL (1,992.401 Da). The bovine hemoglobin P3 ...

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Section: Sequence Characteristicsmentioning

confidence: 99%

“…Recently, we reported the first isolation of P3, a component of the bovine hemoglobin ␣-subunit (15). Its primary sequence is VNFKLLSHSLLVTLASHL (1,992.401 Da).…”

mentioning

confidence: 99%

Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model

Zhang

Wang

et al. 2015

Antimicrob Agents Chemother

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“…Similar results were observed in other studies, as well as with supplementation of Schizochytrium sp. [168,169].…”

Section: Ruminantsmentioning

confidence: 99%

“…Controlled pepsin hydrolysis of haemoglobin yielded the AMPs VLSAADKGNVKAAWGKVGGHAAEYGAEALERMF, ASHLPSDFTPAVHASLDKFLANVSTVLTSKYR and VLSAADKGNVKAAWGKVGGHAAEYGAEAL ERMFLSF. The peptides showed strong inhibition against Salmonella enteritidis, Escherichia coli, Shigella sonnei, Micrococcus luteus, Enterococcus faecalis, Listeria innocua, Staphylococcus saprophyticus, Bacillus cereus and Staphylococcus simulants [168,169].…”

Section: Anti-cancermentioning

confidence: 99%

Food Proteins and Bioactive Peptides

2018

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“…Since the emergence of antibiotic-resistant pathogenic bacteria, the discovery of new AMPs to substitute for traditional antibiotics has become increasingly important [15]. Therefore, in the present study we intended to identify, isolate and characterize AMPs that are synthesized along the epididymis and secreted into the lumen.…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of Molecules Having Anti-microbial Activities from Rabbit Epididymis Using Proteomic Approach

K.V.R¹,

Deva²,

Aranha³

et al. 2011

J Microb Biochem Technol

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Antimicrobial peptides (AMPs) are the key components of the host innate immune system and form the first line of host defense against invading pathogens. In the present study attempts were made to identify and characterize AMPs that are synthesized in the epididymal epithelial cells (EPECs) of rabbit, Oryctologus cuniculus. Ex-vivo induction of EPECs with TLR-9 ligand, CpG-ODN-2006 resulted an up-regulation of several AMPs. These molecules were identified in the acid extracts of pooled epididymal tissue homogenates using proteomic approach (Ultrafiltration, cation-exchange chromatography, RP-HPLC, Far Western blotting -FWB, 2D-PAGE and MALDI-TOF-MS). The pooled RP-HPLC fraction (peaks 1-5), named as rabbit epididymal secretory antimicrobial protein (RESAMP), showed activity against several pathogens. FWB, 2D-PAGE and MALDI-TOF-MS results revealed that of the ~19 proteins identified, four protein sequences (hemoglobin-α/β subunits, transthyretin and calreticulin) found to be reacted with HIV antigens (gp120, gp17, gp41, p24). One of the four sequences (VLSHHFGKEFTPQVQ) showed >90% homology with hemohlobin-β protein. A 29 mer peptide with VLSHHFGKEFTPQVQ sequence designated as rabbit epididymal hemoglobin beta (REHbβP). The synthesized peptide showed the highest Probability Based Mowse Score (PBMS) and demonstrated good bactericidal activity (Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Streptococcus pyogenes and Candida albicans. REHbβP did not show cytotoxicity against human endocervical cells (End1/E6E7) and rabbit erythrocytes. Immunofluorescent results revealed that REHbβP localized in the stereocilia epididymis and on the acrosome of ejaculated spermatozoa of rabbit. To the best our knowledge, this is the first study describing the detection of AMPs in rabbit epididymis. In conclusion, the present study suggests that EPECs derived REHbβP may have therapeutic potential in the management of reproductive well being of human and animals.

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Isolation and characterization of an antimicrobial peptide from bovine hemoglobin α-subunit

Cited by 48 publications

References 13 publications

Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model

Potential of Novel Antimicrobial Peptide P3 from Bovine Erythrocytes and Its Analogs To Disrupt Bacterial Membranes In Vitro and Display Activity against Drug-Resistant Bacteria in a Mouse Model

Food Proteins and Bioactive Peptides

Identification and Characterization of Molecules Having Anti-microbial Activities from Rabbit Epididymis Using Proteomic Approach

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