A Comparison of Bovine Torovirus Strains Based on Partial Membrane Glycoprotein (M) Gene Sequences

A novel coronavirus first broke out in Wuhan, China in December, 2019 has been declared a pandemic by WHO on March, 2020. This work aimed to search for probable ancestor of the virus, phylogeny of 2019-nCoVs and similar SL-CoVs based on the whole genome, M, N, ORF1ab, orf3a, and S gene sequences (n=84) obtained from GenBank using BLASTn software in the NCBI was done. Nucleotides of ORF3a and S-genes among 2019-nCoVs are identical, whereas its similar on the whole genome (99.9-100%), M-gene (99.7-100%), N-gene (99.9-100%) and ORF1ab-gene (99.7-100%). nCoVs are similar to bat CoV/RaTG13 on the whole genome (96.2%), M-gene (95.0%), N-gene (97%), ORF1ab-gene (95.3%), ORF3a-gene (99.1%) and S-gene (90.7%). Likewise, nCoVs exhibited homology to bat-CoVZXC21 on M-gene (93.2%), N-gene (91.5%), ORF1ab-gene (93.1%) and ORF3a-gene (94.4%). The emergent viruses shared identity to bat-CoVZC45 on N-gene (91.3%), ORF1ab-gene (92.8%) and ORF3a-gene (94.0%). In addition, pangolin-CoV/MP789 exhibited common sequences on M-gene (91.0%), N-gene (96.3%) and ORF3a-gene (93.3%) to nCoV. Furthermore, pangolin-CoV/MP789 is analogous to bat CoV/RaTG13 (91.3%) and bat-SL-CoVZXC21 (92.2%) on M-gene and to bat CoV/RaTG13 (94.8%) on N-gene. Nevertheless, nCoVs are distinct from the previously identified SL-CoVs of human origin. The present analysis indicates that nCoVs may have transmitted from bats, pangolin and/or unidentified hosts.

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Prevalence and Distribution of Avian Influenza Viruses in Domestic Ducks at the Waterfowl-Chicken Interface in Wetlands

Pathogens ◽

10.3390/pathogens9110953 ◽

2020 ◽

Vol 9 (11) ◽

pp. 953

Author(s):

Mohammad M. Hassan ◽

Ariful Islam ◽

Rubyath B. Hasan ◽

Md. K. Rahman ◽

Richard J. Webby ◽

...

Keyword(s):

Risk Factors ◽

Phylogenetic Analysis ◽

Avian Influenza ◽

Prevalence Rates ◽

Gene Sequences ◽

M Gene ◽

Domestic Ducks ◽

Free Range ◽

Pathogenic Avian Influenza ◽

Education Status

Ducks are a natural reservoir of influenza A viruses (IAVs) and can act as a reassortment vessel. Wetlands, such as Hakaluki and Tanguar haor in Bangladesh, have unique ecosystems including domestic duck (Anas platyrhynchos domesticus) rearing, especially household and free-range ducks. A cross-sectional study was, therefore, conducted to explore avian influenza status and its distribution and risk factors in the wetland areas. During the three consecutive winters of 2015–2017, specifically in December of these years, we collected a total of 947 samples including blood, oropharyngeal and cloacal swabs from domestic ducks (such as free-range ducks (n = 312 samples) and household ducks (n = 635 samples) in wetlands. We screened serum samples using a nucleoprotein competitive enzyme-linked immunosorbent assay (c-ELISA) to estimate seroprevalence of IAV antibodies and swab samples by real-time reverse transcriptase polymerase chain reaction (rRT-PCR) to detect IA viral M gene. Eleven M gene positive samples were subjected to sequencing and phylogenetic analysis. Serological and viral prevalence rates of IAVs were 63.8% (95% CI: 60.6–66.8) and 10.7% (8.8–12.8), respectively. Serological and viral RNA prevalence rates were 51.8% (95% CI: 47.2–56.4) and 10.2% (7.6–13.3) in Hakaluki haor, 75.6% (71.5–79.4) and 11.1% (8.5–14.3) in Tanguar haor, 66.3% (62.5–69.9) and 11.2% (8.8–13.9) in household ducks and 58.7% (52.9–64.2) and 9.6% (6.5–13.4) in free-range ducks, respectively. The risk factors identified for higher odds of AI seropositive ducks were location (OR = 2.9, 95% CI: 2.2–3.8, p < 0.001; Tanguar haor vs. Hakaluki haor), duck-rearing system (OR = 1.4, 1.1–1.8, household vs. free-range), farmer’s education status (OR = 1.5, 1.2–2.0, p < 0.05 illiterate vs. literate) and contact type (OR = 3.0, 2.1–4.3, p < 0.001; contact with chicken vs. no contact with chicken). The risk factors identified for higher odds of AI viral RNA positive ducks were farmer’s education status (OR = 1.5, 1.0–2.3, p < 0.05 for illiterate vs literate), contact type (OR = 2.7, 1.7–4.2, p < 0.001; ducks having contact with chicken vs. ducks having contact with waterfowl). The phylogenetic analysis of 11 partial M gene sequences suggested that the M gene sequences detected in free-range duck were very similar to each other and were closely related to the M gene sequences of previously reported highly pathogenic avian influenza (HPAI) and low pathogenic avian influenza (LPAI) subtypes in waterfowl in Bangladesh and Southeast Asian countries. Results of the current study will help provide significant information for future surveillance programs and model IAV infection to predict the spread of the viruses among migratory waterfowl, free-range ducks and domestic poultry in Bangladesh.

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Distribution of the SsuDAT1I Restriction-Modification System among Different Serotypes ofStreptococcus suis

Journal of Bacteriology ◽

10.1128/jb.183.18.5436-5440.2001 ◽

2001 ◽

Vol 183 (18) ◽

pp. 5436-5440 ◽

Cited By ~ 12

Author(s):

Tsutomu Sekizaki ◽

Makoto Osaki ◽

Daisuke Takamatsu ◽

Yoshihiro Shimoji

Keyword(s):

Genetic Divergence ◽

Field Isolate ◽

Gene Sequences ◽

M Gene ◽

Recognition Sequence ◽

Modification System ◽

Restriction Modification System ◽

Serotype 1 ◽

Reference Strains ◽

Restriction Modification

ABSTRACT The SsuDAT1I restriction-modification (R-M) system, which contains two methyltransferases and two restriction endonucleases with recognition sequence 5′-GATC-3′, was first found in a field isolate of Streptococcus suis serotype 2. Isoschizomers of the R-M system were found in the same locus betweenpurH and purD in a field isolate of serotype 1/2 and the reference strains of serotypes 3, 7, 23, and 26 among 29 strains of different serotypes examined in this study. The R-M gene sequences in serotypes 1/2, 3, 7, and 23 were very similar to those of SsuDAT1I, whereas those in serotype 26 were less similar. These results indicate intraspecies recombination among them and genetic divergence through their evolution.

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Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647026 ◽

1988 ◽

Vol 60 (02) ◽

pp. 182-187 ◽

Cited By ~ 2

Author(s):

Morio Aihara ◽

Ken Tamura ◽

Ryuko Kawarada ◽

Keizou Okawa ◽

Yutaka Yoshida

Keyword(s):

Platelet Aggregation ◽

Von Willebrand Factor ◽

Ricinus Communis ◽

Protein S ◽

Platelet Membrane ◽

Membrane Glycoprotein ◽

Normal Plasma ◽

Ricinus Communis Agglutinin ◽

Von Willebrand ◽

Willebrand Factor

SummaryThe adhesion of human fixed washed platelets (FWP) to collagen was decreased after treatment with Serratia marcescens protease (SP), which removed 95% of the glycocalicin from platelet membrane glycoprotein (GP) lb. However, the diminished adhesion of SP treated FWP to collagen could still be increased in the presence of purified von Willebrand factor (vWF). This ability of vWF to increase FWP adhesion to collagen is defined as collagen cofactor (CCo). The adhesion of FWP to collagen was not affected by a monoclonal antibody (MAb) to GP Ilb/IIIa (10E5), that inhibits ADP and collagen induced platelet aggregation. On the other hand, it was decreased by 50% by a MAb to GP lb (6D1), that inhibits ristocetin induced platelet aggregation. Adhesion of FWP in buffer to collagen was completely inhibited by Ricinus communis agglutinin I or concanavalin A, while Lens culinalis agglutinin and wheat germ agglutinin showed 50% inhibition. The FWP adhesion to collagen in the presence of vWF (normal plasma) was unaffected by MAbs to GP Ilb/IIIa (10E5, P2, HPL1) but was decreased to 32-38% by MAbs to GP lb (6D1, AN51, HPL11). A MAb to vWF (CLB-RAg 35), that inhibits ristocetin induced binding of vWF to platelets, decreased the CCo of normal plasma by 70%. The MAb, CLB-RAg 201, that inhibits the binding of vWF to collagen, completely inhibited the CCo of normal plasma. In conclusion, our data suggest that (1) GP lb has a partial role in FWP adhesion to collagen; (2) the binding of vWF to collagen is required for the expression of CCo; (3) CCo is partly mediated through GP lb; but (4) other platelet membrane protein(s) besides GP lb or GP Ilb/IIIa must also be involved in FWP-vWF-collagen interactions.

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Ristocetin and Botrocetin Involve Two Distinct Domains of von Willebrand Factor for Binding to Platelet Membrane Glycoprotein lb

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647310 ◽

1990 ◽

Vol 64 (02) ◽

pp. 326-332 ◽

Cited By ~ 57

Author(s):

J P Girma ◽

Y Takahashi ◽

A Yoshioka ◽

J Diaz ◽

D Meyer

Keyword(s):

Von Willebrand Factor ◽

Synthetic Peptides ◽

Competitive Inhibition ◽

Final Concentration ◽

Binding Domain ◽

Platelet Membrane ◽

Platelet Glycoprotein ◽

Membrane Glycoprotein ◽

Von Willebrand ◽

Willebrand Factor

SummaryWe have evidence that ristocetin and botrocetin mediate binding of von Willebrand Factor (vWF) to platelet glycoprotein lb (GPIb) through two distinct domains on the vWF molecule. This was established by using monoclonal antibodies (MAbs) to vWF and synthetic peptides derived from the sequence of vWF. MAb 322 and MAb NMC/vW 4 both recognize native vWF as well as fragments containing the GPIb-binding domain of vWF, obtained with the following enzymes: trypsin (116 kDa), V-8 pro tease (Spill, 320 kDa) and V-8 protease plus subtilisin (33-28 kDa). Nevertheless, the lack of reciprocal displacement between the two MAbs in experiments of competitive inhibition for binding to vWF demonstrate that their respective epitopes are separate. Both MAbs inhibit 125I-vWF binding to platelet membrane GPIb and vWF-dependent platelet agglutination induced by ristocetin. However, only MAb NMC/vW4 inhibits these functions in the presence of botrocetin and when ristocetin-induced platelet agglutination is inhibited by MAb 322, botrocetin is still able to restore the agglutination. The involvement of two distinct domains of vWF for binding to GPIb in the presence of ristocetin or botrocetin was confirmed in experiments of binding of 125I-vWF to platelets using as competitor synthetic peptides corresponding to the GPIb binding domain of vWF (Cys 474 to Pro 488 and Ser 692 to Pro 708). At a final concentration of 2.5 mM both peptides inhibit more than 90% of the binding of vWF to ristocetin-treated platelets but are unable to modify this binding in the presence of botrocetin. In conclusion our data suggest that botrocetin and ristocetin involve distinct sites on vWF for binding to GPIb.

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Responses of Platelets to Strains of Streptococcus sanguis: Findings in Healthy Subjects, Bernard-Soulier, Glanzmann’s, and Collagen-Unresponsive Patients

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651098 ◽

1987 ◽

Vol 57 (02) ◽

pp. 222-225 ◽

Cited By ~ 19

Author(s):

A H Soberay ◽

M C Herzberg ◽

J D Rudney ◽

H K Nieuwenhuis ◽

J J Sixma ◽

...

Keyword(s):

Platelet Aggregation ◽

Healthy Subjects ◽

Normal Subjects ◽

Membrane Glycoprotein ◽

Response Mechanism ◽

Platelet Response ◽

Induce Platelet Aggregation ◽

Streptococcus Sanguis ◽

Lag Times ◽

Bernard Soulier Syndrome

SummaryThe ability of endocarditis and dental strains of Streptococcus sanguis to induce platelet aggregation in plasma (PRP) from normal subjects were examined and compared to responses of PRP with known platelet membrane glycoprotein (GP) and response defects. S. sanguis strains differed in their ability to induce normal PRPs to aggregate. Strains that induced PRP aggregation in more than 60% of donors were significantly faster agonists (mean lag times to onset of aggregation less than 6 min) than those strains inducing response in PRPs of fewer than 60% of donors.Platelets from patients with Bernard-Soulier syndrome aggregated in response to strains of S. sanguis. In contrast, platelets from patients with Glanzmann’s thrombasthenia and from a patient with a specific defect in response to collagen were unresponsive to S. sanguis. These observations show that GPIb and V are not essential, but GPIIb-IIIa and GPIa are important in the platelet response mechanism to S. sanguis. Indeed, the data suggests that the platelet interaction mechanisms of S. sanguis and collagen may be similar.

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Acquired Disorder of Platelet Function Associated with Autoantibodies against Membrane Glycoprotein IIb-IIIa Complex - 1. Glycoprotein Analysis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648178 ◽

1991 ◽

Vol 65 (05) ◽

pp. 491-496 ◽

Cited By ~ 29

Author(s):

M Meyer ◽

C M Kirchmaier ◽

A Schirmer ◽

P Spangenberg ◽

Ch Ströhl ◽

...

Keyword(s):

Platelet Count ◽

Platelet Aggregation ◽

Platelet Adhesion ◽

Bleeding Time ◽

Membrane Glycoprotein ◽

Membrane Glycoproteins ◽

Abnormal Behaviour ◽

Thrombocytopenic Purpura ◽

Immunoelectrophoretic Analysis ◽

Prolonged Bleeding Time

SummaryA patient with idiopathic thrombocytopenic purpura developed after splenectomy a thrombasthenia-like severe haemor-rhagic diathesis characterized by a normal or subnormal platelet count, prolonged bleeding time, strongly reduced platelet adhesion to glass and defective platelet aggregation in response to ADP and collagen. In contrast to hereditary thrombasthenia membrane glycoproteins (GP) lib and Ilia were normally present in the patient’s platelets. Immunoelectrophoretic analysis revealed an abnormal behaviour of the patient’s GP IIb-IIIa complex. Autoantibodies against GP IIb-IIIa were detected in Triton-extracted washed platelets. Incubation of normal platelets with plasma from the patient resulted in a similar immunoelectrophoretic abnormality of the GP IIb-IIIa complex indicating that bound autoantibodies (IgG) are responsible for the abnormal immunoelectrophoretic behaviour of the patient’s GP IIb-IIIa complex. Platelet fibrinogen was severely reduced similar to classical thrombasthenia suggesting that the GP IIb-IIIa complex is involved in platelet fibrinogen storage.

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Differential Ability of Agonists to Express Distinct Pools of Fibrinogen (Gpllb/llla) Receptors which Can Mediate the Aggregation of Human Platelets

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651035 ◽

1989 ◽

Vol 62 (03) ◽

pp. 955-961 ◽

Cited By ~ 4

Author(s):

Ian S Watts ◽

Rebecca J Keery ◽

Philip Lumley

Keyword(s):

Platelet Aggregation ◽

Human Platelet ◽

Surface Membrane ◽

Blood Platelet ◽

Human Platelets ◽

Membrane Glycoprotein ◽

Platelet Surface ◽

Human Platelet Aggregation ◽

Differential Ability ◽

Blood Platelet Aggregation

SummaryWe have investigated the effect of two procedures that modify human platelet surface membrane glycoprotein (Gp) IIb and IIIa complexes upon whole blood platelet aggregation to a range of agonists. (A) Irreversible disruption of complexes by temporary (30 min) Ca2+-deprivation with EGTA at 37° C. (B) Binding of a monoclonal antibody M148 to the complex. EGTA exposure abolished aggregation to ADP, adrenaline and PAF. In contrast, full aggregation curves to collagen and U-46619 could still be established. EGTA exposure reduced M148 binding to platelets by 80%. Excess M148 abolished aggregation to ADP, PAF, collagen and U-46619. However, upon removal of unbound antibody from platelets full aggregation curves to collagen and U-46619 but not to ADP and PAF could be re-established. Thus human platelet aggregation to ADP, PAF and adrenaline appears absolutely dependent upon surface membrane GpIIb/IIIa complexes. In contrast, collagen and U-46619 cause expression of an additional distinct pool of Gp complexes inaccessible to EGTA and M148 in unstimulated platelets which is intimately involved in aggregation to these agonists.

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Molecular Basis and Clinical Aspects of Hereditary Megakaryocyte and Platelet Membrane Glycoprotein Disorders

Hämostaseologie ◽

10.1055/s-0038-1656647 ◽

1996 ◽

Vol 16 (02) ◽

pp. 114-138 ◽

Cited By ~ 6

Author(s):

R. E. Scharf

Keyword(s):

Genetic Basis ◽

Molecular Mechanisms ◽

Molecular Genetic ◽

Platelet Membrane ◽

Clinical Aspects ◽

Membrane Glycoprotein ◽

Membrane Glycoproteins ◽

Membrane Expression ◽

Receptor Complexes ◽

Platelet Membrane Glycoprotein

SummarySpecific membrane glycoproteins (GP) expressed by the megakaryocyte-platelet system, including GPIa-lla, GPIb-V-IX, GPIIb-llla, and GPIV are involved in mediat-ing platelet adhesion to the subendothelial matrix. Among these glycoproteins, GPIIb-llla plays a pivotal role since platelet aggregation is exclusively mediated by this receptor and its interaction with soluble macromolecular proteins. Inherited defects of the GPIIb-llla or GPIb-V-IX receptor complexes are associated with bleeding disorders, known as Glanzmann's thrombasthenia, Bernard-Soulier syndrome, or platelet-type von Willebrand's disease, respectively. Using immuno-chemical and molecular biology techniques, rapid advances in our understanding of the molecular genetic basis of these disorders have been made during the last few years. Moreover, analyses of patients with congenital platelet membrane glycoprotein abnormalities have provided valuable insights into molecular mechanisms that are required for structural and functional integrity, normal biosynthesis of the glycoprotein complexes and coordinated membrane expression of their constituents. The present article reviews the current state of knowledge of the major membrane glycoproteins in health and disease. The spectrum of clinical bleeding manifestations and established diagnostic criteria for each of these dis-orders are summarized. In particular, the variety of molecular defects that have been identified so far and their genetic basis will be discussed.

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Human Blood Platelet Membrane Glycoproteins

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657050 ◽

1979 ◽

Vol 42 (05) ◽

pp. 1490-1502 ◽

Cited By ~ 3

Author(s):

C S P Jenkins ◽

E F Ali-Briggs ◽

G T E Zonneveld ◽

A Sturk ◽

J Clemetson

Keyword(s):

Specific Problem ◽

Sodium Dodecyl ◽

Normal Subjects ◽

Blood Platelet ◽

Platelet Membrane ◽

Buffer System ◽

Membrane Glycoprotein ◽

Membrane Glycoproteins ◽

Human Blood Platelet ◽

Electrophoretic Techniques

SummaryThe separation of the major platelet membrane glycoproteins of normal subjects and subjects with well defined platelet membrane glycoprotein abnormalities have been examined using four different polyacrylamide gel electrophoretic techniques (continuous and discontinuous). The mobilities of the resolved glycoprotein bands have been correlated with the glycoprotein nomenclature proposed for the conventional sodium dodecyl sulphate- phosphate buffer system. Since the glycoprotein distribution varies depending on the system used, the merits of each method should be considered before application to a specific problem.

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