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Article ; Online: Natural resources to control COVID-19

Ehab H. Mattar / Fatma Elrashdy / Hussein A. Almehdar / Vladimir N. Uversky / Elrashdy M. Redwan

PeerJ, Vol 9, p e

could lactoferrin amend SARS-CoV-2 infectivity?

2021 Volume 11303

Abstract: The world population is still facing the second wave of the COVID-19 pandemic. Such a challenge requires complicated tools to control, namely vaccines, effective cures, and complementary agents. Here we present one candidate for the role of an effective ... ...

Abstract	The world population is still facing the second wave of the COVID-19 pandemic. Such a challenge requires complicated tools to control, namely vaccines, effective cures, and complementary agents. Here we present one candidate for the role of an effective cure and/or complementary agent: lactoferrin. It is the cross-talking mediator between many organs/cellular systems in the body. It serves as a physiological, immunological, and anti-microbial barrier, and acts as a regulator molecule. Furthermore, lactoferrin has receptors on most tissues cells, and is a rich source for bioactive peptides, particularly in the digestive system. In the past months, in vitro and in vivo evidence has accumulated regarding lactoferrin’s ability to control SARS-CoV-2 infectivity in different indicated scenarios. Also, lactoferrin or whey milk (of human or other mammal’s origin) is a cheap, easily available, and safe agent, the use of which can produce promising results. Pharmaceutical and/or food supplementary formulas of lactoferrin could be particularly effective in controlling the gastrointestinal COVID-19-associated symptoms and could limit the fecal-oral viral infection transmission, through mechanisms that mimic that of norovirus infection control by lactoferrin via induction of intestinal innate immunity. This natural avenue may be effective not only in symptomatic patients, but could also be more helpful in asymptomatic patients as a main or adjuvant treatment.
Keywords	Lactoferrin ; COVID-19 ; SARS-CoV-2 ; Multifunctional protein ; Medicine ; R
Language	English
Publishing date	2021-04-01T00:00:00Z
Publisher	PeerJ Inc.
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Yield and Composition Variations of the Milk from Different Camel Breeds in Saudi Arabia

Amr A. El-Hanafy / Yasser M. Saad / Saleh A. Alkarim / Hussein A. Almehdar / Fuad M. Alzahrani / Mohammed A. Almatry / Vladimir N. Uversky / Elrashdy M. Redwan

Sci, Vol 5, Iss 2, p

2023 Volume 2

Abstract: With the increasing interest in the identification of differences between camel breeds over the last decade, this study was conducted to estimate the variability of milk production and composition of four Saudi camel breeds during different seasons. Milk ...

Abstract	With the increasing interest in the identification of differences between camel breeds over the last decade, this study was conducted to estimate the variability of milk production and composition of four Saudi camel breeds during different seasons. Milk records were taken two days per week from females of Majahem, Safra, Wadha, and Hamra breeds distributed over Saudi Arabia. The milk yield during winter indicated that the weekly average of the Wadha breed was significantly lower (27.13 kg/week) than Majahem and Hamra breeds. The Safra breed had the lowest milk yield (30.7 kg/week) during summer. During winter, the Hamra breed had a lower content of all analyzed milk components except proteins and was characterized by a lower pH than the milk of the other breeds. However, the Hamra breed had significantly higher contents of milk fat and lactose than the other breeds during summer, with the corresponding values of 3.87 and 4.86%, respectively. Milk collected during winter from Majahem, Safra, and Wadha breeds was characterized by a significant increase in all milk components and milk pH. Finally, the isoelectric focusing analysis revealed noticeable variability of casein purified from camel milk within the different Saudi breeds, with the highest significant value of 2.29 g per 100 mL recorded for the Wadha breed.
Keywords	breed ; camel ; clan ; milk composition ; milk production ; Saudi Arabia ; Science ; Q
Subject code	630
Language	English
Publishing date	2023-01-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Exploring the mechanisms by which camel lactoferrin can kill Salmonella enterica serovar typhimurium and Shigella sonnei

Hussein A. Almehdar / Nawal Abd El-Baky / Ehab H. Mattar / Raed Albiheyri / Atif Bamagoos / Abdullah Aljaddawi / Vladimir N. Uversky / Elrashdy M. Redwan

PeerJ, Vol 11, p e

2023 Volume 14809

Abstract: There is a continuously increasing pressure associated with the appearance of Salmonella enterica Serovar typhimurium (S. typhimurium) and Shigella sonnei (S. sonnei) that have developed pathogenic multiple antibiotic resistance and the cost of cure and ... ...

Abstract	There is a continuously increasing pressure associated with the appearance of Salmonella enterica Serovar typhimurium (S. typhimurium) and Shigella sonnei (S. sonnei) that have developed pathogenic multiple antibiotic resistance and the cost of cure and control of these enterobacteriaceae infections increases annually. The current report for first time demonstrated the distinguished antimicrobial action of camel lactoferrin (cLf) obtained from the milk of different clans of camel in Saudi Arabia against S. typhimurium and S. sonnei. These cLf subtypes showed comparable antimicrobial potential when tested against the two bacterial strains but were superior to either bovine (bLf) or human lactoferrin (hLf). The synergism between lactoferrins and antibiotics concerning their antibacterial efficacies against the two bacterial strains was evident. Exploring mechanisms by which camel lactoferrin can kill S. typhimurium and S. sonnei revealed that cLf affects bacterial protein profile. Besides, it interacts with bacterial lipopolysaccharides (LPS) and numerous membrane proteins of S. typhimurium and S. sonnei, with each bacterial strain possessing distinctive binding membrane proteins for lactoferrin. Furthermore, as evidenced by electron microscopy analysis, cLf induces extracellular and intracellular morphological changes in the test bacterial strains when used alone or in combination treatment with antibiotics. Lactoferrin and antibiotics combination strongly disrupts the integrity of the bacterial cells and their membranes. Therefore, cLf can kill S. typhimurium and S. sonnei by four different mechanisms, such as iron chelation, affecting some bacterial proteins, binding to bacterial LPS and membrane proteins, and impairing the integrity of the bacterial cells and their membranes.
Keywords	Camel milk ; Lactoferrin ; Antibacterial ; Salmonella typhimurium ; Shigella sonnei ; Medicine ; R ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2023-01-01T00:00:00Z
Publisher	PeerJ Inc.
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Comparative Analysis of Milk Fat Globular Membrane (MFGM) Proteome between Saudi Arabia Camelus dromedary Safra and Wadha Breeds

Bassam H. Sabha / Afshan Masood / Ibrahim O. Alanazi / Assim A. Alfadda / Hussein A. Almehdar / Hicham Benabdelkamel / Elrashdy M. Redwan

Molecules, Vol 25, Iss 2146, p

2020 Volume 2146

Abstract: Camel milk is traditionally known to have medicinal properties and many potential health benefits. Natural milk contains many soluble proteins and nanoparticles, such as a milk fat globule membrane (MFGM), a three-layered membrane covering of milk fat ... ...

Abstract	Camel milk is traditionally known to have medicinal properties and many potential health benefits. Natural milk contains many soluble proteins and nanoparticles, such as a milk fat globule membrane (MFGM), a three-layered membrane covering of milk fat globule mainly composed of proteins and lipids, which plays an important role in human health. MFGM proteins account for 1%–4% of total milk proteins, and their nutritive value and distribution depends on the different breeds. The differential composition of these membrane proteins among different camel breeds has not been explored. The current study, therefore, aimed to quantitatively analyze and compare the MFGM proteome between the milk produced by the two most common Saudi camel breeds, Camelus dromedarius : Safra and Wadha. Two-dimensional difference in gel electrophoresis (2D-DIGE) and mass spectrometry analysis revealed a total of 44 MFGM proteins that were identified with a significant difference in abundance ( p ≤ 0.05; fold change ≥ 1.5) between the two breeds. Thirty-one proteins were up-regulated and 13 proteins were down-regulated in the Safra breed compared to the Wadha breed. The proteins identified with an increased abundance included α-lactalbumin, lactadherin, and annexin a8, whereas the down-regulated proteins included butyrophilin subfamily 1 member a1, lactotransferrin, and vinculin. The differentially abundant proteins were analyzed by the UNIPROT system and gene ontology (GO) to reveal their associations with known biological functions and pathways. Enzyme-linked immunosorbent assay (ELISA) confirmed the 2D-DIGE findings of butyrophilin (BTN) and α-lactalbumin (α-LA) levels obtained from Safra and Wadha breeds.
Keywords	Safra breed ; Wadha breed ; camel milk ; proteomics ; 2D-DIGE ; MFGM ; Organic chemistry ; QD241-441
Subject code	630
Language	English
Publishing date	2020-05-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Prediction of Disordered Regions and Their Roles in the Anti-Pathogenic and Immunomodulatory Functions of Butyrophilins

Elrashdy M. Redwan / Ahmed M. Al-Hejin / Hussein A. Almehdar / Abdelrahman M. Elsaway / Vladimir N. Uversky

Molecules, Vol 23, Iss 2, p

2018 Volume 328

Abstract: Butyrophilins (BTNs) are a group of the moonlighting proteins, some members of which are secreted in milk. They constitute a large family of structurally similar type 1 transmembrane proteins from the immunoglobulin superfamily. Although the founding ... ...

Abstract	Butyrophilins (BTNs) are a group of the moonlighting proteins, some members of which are secreted in milk. They constitute a large family of structurally similar type 1 transmembrane proteins from the immunoglobulin superfamily. Although the founding member of this family is related to lactation, participating in the secretion, formation and stabilization of milk fat globules, it may also have a cell surface receptor function. Generally, the BTN family members are known to modulate co-stimulatory responses, T cell selection, differentiation, and cell fate determination. Polymorphism of these genes was shown to be associated with the pathology of several human diseases. Despite their biological significance, structural information on human butyrophilins is rather limited. Based on their remarkable multifunctionality, butyrophilins seem to belong to the category of moonlighting proteins, which are known to contain intrinsically disordered protein regions (IDPRs). However, the disorder status of human BTNs was not systematically investigated as of yet. The goal of this study is to fill this gap and to evaluate peculiarities of intrinsic disorder predisposition of the members of human BTN family, and to find if they have IDPRs that can be attributed to the multifunctionality of these important proteins.
Keywords	butyrophilin ; structure ; function ; immune response ; antigen presentation ; intrinsic disorder ; Organic chemistry ; QD241-441
Subject code	570
Language	English
Publishing date	2018-02-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Publisher Correction

Essam J. Alyamani / Sarah A. Marcus / Sarah M. Ramirez-Busby / Chungyi Hansen / Julien Rashid / Amani El-kholy / Daniel Spalink / Faramarz Valafar / Hussein A. Almehdar / Asif A. Jiman-Fatani / Mohamed A. Khiyami / Adel M. Talaat

Scientific Reports, Vol 9, Iss 1, Pp 1-

Genomic analysis of the emergence of drug-resistant strains of Mycobacterium tuberculosis in the Middle East

2019 Volume 1

Abstract: An amendment to this paper has been published and can be accessed via a link at the top of the paper. ...

Abstract	An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2019-12-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Genomic analysis of the emergence of drug-resistant strains of Mycobacterium tuberculosis in the Middle East

Scientific Reports, Vol 9, Iss 1, Pp 1-

2019 Volume 12

Abstract: Abstract Tuberculosis (TB) represents a significant challenge to public health authorities, especially with the emergence of drug-resistant (DR) and multidrug-resistant (MDR) isolates of Mycobacterium tuberculosis. We sought to examine the genomic ... ...

Abstract	Abstract Tuberculosis (TB) represents a significant challenge to public health authorities, especially with the emergence of drug-resistant (DR) and multidrug-resistant (MDR) isolates of Mycobacterium tuberculosis. We sought to examine the genomic variations among recently isolated strains of M. tuberculosis in two closely related countries with different population demography in the Middle East. Clinical isolates of M. tuberculosis from both Egypt and Saudi Arabia were subjected to phenotypic and genotypic analysis on gene and genome-wide levels. Isolates with MDR phenotypes were highly prevalent in Egypt (up to 35%) despite its relatively stable population structure (sympatric pattern). MDR-TB isolates were not identified in the isolates from Saudi Arabia despite its active guest worker program (allopatric pattern). However, tuberculosis isolates from Saudi Arabia, where lineage 4 was more prevalent (>65%), showed more diversity than isolates from Egypt, where lineage 3 was the most prevalent (>75%). Phylogenetic and molecular dating analyses indicated that lineages from Egypt were recently diverged (~78 years), whereas those from Saudi Arabia were diverged by over 200 years. Interestingly, DR isolates did not appear to cluster together or spread more widely than drug-sensitive isolates, suggesting poor treatment as the main cause for emergence of drug resistance rather than more virulence or more capacity to persist.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2019-03-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Chicken cathelicidins as potent intrinsically disordered biocides with antimicrobial activity against infectious pathogens

Yacoub, Haitham A / Ahmed M. Elazzazy / Ekram S. Ahmed / Hussein A. Almehdar / Maged M. Mahmoud / Mohamed Nabih Baeshen / Omar A. Al-Maghrabi / Saleh Alkarim / Vladimir N. Uversky

Developmental and comparative immunology. 2016 Dec., v. 65

2016

Abstract: This study was performed to identify the expression patterns of the cathelicidin genes in a local chicken breed and to evaluate the antimicrobial activities of the cathelicidin peptides against pathogenic bacteria. This analysis revealed that the coding ... ...

Abstract	This study was performed to identify the expression patterns of the cathelicidin genes in a local chicken breed and to evaluate the antimicrobial activities of the cathelicidin peptides against pathogenic bacteria. This analysis revealed that the coding regions of CATH-1, -2, and -3 genes contain 447 bp, 465 bp, and 456 bp, respectively, and encode proteins of 148, 154, 151 amino acids, respectively. The complete amino acid sequences of the cathelicidin peptides are similar to those found in Meleagris gallopavo, Phasianus colchicus, and Coturnix coturnix, and show high sequence identity to their Columba livia and Anas platyrhynchos counterparts. In contrast, these avian peptides shared a very low sequence identity with the mammalian cathelicidins. The analysis further revealed that the cathelicidin genes are expressed in various organ and tissues. We also show that the CATH peptides 1, 2, 3 and their amide-modified structures possess potent antimicrobial activities against both Gram-positive and Gram-negative pathogens, with these bacteria being affected to different extents. The antimicrobial activities of the peptides are slightly lower than those of their amide analogs. Computational analysis revealed that pre-pro-cathelicidins are hybrid proteins that contain ordered domains and functional intrinsically disordered regions. Furthermore, high structural and sequence variability of mature cathelicidins is a strong indication of their rather disordered nature. It is likely that intrinsic disorder is needed for the multifarious functionality of these antimicrobial peptides. Our analyses indicated that cathelicidin peptides require further study to better understand their full potentials in the treatment of diseases in both humans and animals. The data obtained for synthetic avian peptides will help elucidating of their potential applications in the pharmaceutical industry.
Keywords	amino acid sequences ; amino acids ; Anas platyrhynchos ; bacteria ; cathelicidins ; chickens ; Columba livia ; Coturnix coturnix ; gene expression ; genes ; genetic variation ; immune response ; Meleagris gallopavo ; pathogens ; Phasianus colchicus ; proteins ; sequence analysis
Language	English
Dates of publication	2016-12
Size	p. 8-24.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	752411-0
ISSN	1879-0089 ; 0145-305X
ISSN (online)	1879-0089
ISSN	0145-305X
DOI	10.1016/j.dci.2016.06.012
Database	NAL-Catalogue (AGRICOLA)

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Article: Significant antibacterial activity and synergistic effects of camel lactoferrin with antibiotics against methicillin-resistant Staphylococcus aureus (MRSA)

Redwan, Elrashdy M / Abdulrahman Elsaway / Abu-Bakr M. Gomaa / Ahmed M. Al-Hejin / Fahad A. Al-Fassi / Hussein A. Almehdar / Isam Eldin AbuZeid / Mohammed N. Baeshen / Nawal Abd El-Baky / Saad Berki Al-Masaudi / Vladimir N. Uversky

Institut Pasteur Research in microbiology. 2016 July, Aug., v. 167, no. 6

2016

Abstract: Methicillin-resistant Staphylococcus aureus (MRSA) causes major healthcare problems in many countries, as it is present as several hospital- and community-associated strains. Hospital-associated MRSA is one of the most prevalent nosocomial pathogens ... ...

Abstract	Methicillin-resistant Staphylococcus aureus (MRSA) causes major healthcare problems in many countries, as it is present as several hospital- and community-associated strains. Hospital-associated MRSA is one of the most prevalent nosocomial pathogens throughout the world and infections caused by community-acquired MRSA are rising. This emphasizes the need for new and efficient anti-MRSA agents. We evaluated the antibacterial effects of camel lactoferrin (cLf) and human lactoferrin (hLf) alone and in combination with several antibiotics against MRSA. Antimicrobials were tested against MRSA and an S. aureus control strain by the agar disc diffusion method. The minimum inhibitory concentration (MIC) was determined for antimicrobials by the broth microdilution method. Synergy between cLf or hLf and antibiotics was examined by checkerboard and time-kill assays. The agar disc diffusion assay showed that MRSA growth was inhibited by cLf at 0.25–3 mg/ml and hLf at 1–3 mg/ml. cLf demonstrated 3 times higher inhibitory activity against MRSA than hLf in terms of MIC values (250 vs. 750 μg/ml, respectively). Biotinylated cLf was recognized by two membrane proteins of MRSA, 66–67 KDa. Combinations of cLf or hLf and oxacillin or vancomycin at sub-MIC levels enhanced in vitro antibacterial activity against MRSA compared with each agent alone.
Keywords	antibacterial properties ; antibiotic resistance ; camels ; cross infection ; health services ; humans ; lactoferrin ; membrane proteins ; methicillin ; methicillin-resistant Staphylococcus aureus ; minimum inhibitory concentration ; oxacillin ; pathogens ; synergism ; vancomycin
Language	English
Dates of publication	2016-07
Size	p. 480-491.
Publishing place	Elsevier Masson SAS
Document type	Article
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2016.04.006
Database	NAL-Catalogue (AGRICOLA)

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