Howard L. Bachrach

Plum Island Animal Disease Center

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Jerome Polatnick

Plum Island Animal Disease Center

S. S. Breese

Plum Island Animal Disease Center

P. D. McKercher

Plum Island Animal Disease Center

W. R. Hess

Information Technology Laboratory

George F. Vande Woude

Van Andel Institute

J. J. Callis

University of Kent

Marvin J. Grubman

Plum Island Animal Disease Center

Rodes Trautman

University of Western Australia

Barry Baxt

Plum Island Animal Disease Center

H. D. Matheka

Max Planck Institute for Biology

Cooperative Institutions

Plum Island Animal Disease Center

United States Department of Agriculture

Agricultural Research Service

National Institutes of Health

Baylor College of Medicine

National Cancer Institute

Cornell University

University of California, Berkeley

Cancer Research Center

Centers for Disease Control and Prevention

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Visualization by chilling of protein bands in polyacrylamide gels containing 8 m urea: Preparation and quantitation of foot-and-mouth disease virus capsid proteins

Analytical Biochemistry (1981)

Howard L. Bachrach

Polyacrylamide

Coomassie Brilliant Blue

Absorbance

Bradford protein assay

10.1016/0003-2697(81)90202-5

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Citations (7)

Purification studies on Lansing poliomyelitis virus. II. Analytical electron microscopic identification of the infectious particle in preparations of high specific infectivity.

PubMed (1954)

Howard L. Bachrach C. E. Schwerdt

The virus in the concentrates of high specific infectivity has been identified by analytical electron microscopy to be a spherical particle 28 mμ in diameter. This identification was made through correlative experiments relating particle counts to infectivity and is discussed in detail. The concentration of the virus in CNS tissue of paralytic cotton rats is calculated to be about 0.2 μg per gram of tissue. It is shown that about 21,000 virus particles or 3.0 × 10-13 g of virus are consistently present in one LD50 inoculum for cotton rats, but it is not known whether all or a constant fraction of these particles are infectious. The electron microscopic evidence shows that the virus is highly uniform in size and shape.

Infectivity

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Citations (37)

Rotational Symmetry in Foot-and-Mouth Disease Virus and Models

Science (1965)

S. S. Breese Rodes Trautman Howard L. Bachrach

With small, animal viruses for which electron-microscope images show little penetration by negative stain, the rotation technique for structure determination is useful. Foot-and-mouth disease virus resembles a 32-unit model when rotational images of virus and models simulating virus in negative stain are compared.

Stain

Penetration (warfare)

Negative stain

10.1126/science.150.3701.1303

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Citations (17)

Comparative Strategies of Animal Virus Replication

Advances in virus research (1978)

Howard L. Bachrach

Replication

10.1016/s0065-3527(08)60774-5

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Citations (15)

Varia

Intervirology (1979)

Howard L. Bachrach Donald O. Morgan Douglas M. Moore Eng‐Chun Mar Eng‐Shang Huang

10.1159/000149080

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Citations (1)

Quantitation of the Antigenicity and Immunogenicity of Purified Foot-and-Mouth Disease Virus Vaccine for Swine and Steers

Applied Microbiology (1970)

D.O. Morgan P. D. McKercher Howard L. Bachrach

The antigenicity and immunogenicity of a purified preparation of foot-and-mouth disease virus [type A 12 , strain 119 (FMDV A-119)] inactivated with 6.0 m m N -acetylethylenimine at 37 C were compared in swine and steers. Three antigen doses were tested, 640, 160, and 40 ng. In accordance with findings for guinea pigs, as previously determined by dose-response curves, as little as fourfold changes in antigen in the region of the minimum effective dose produced marked differences in the serological and immune responses of swine. The minimum effective dose of antigen for antibody formation in swine and guinea pigs, as determined by mouse median protective dose (PD 50 ) values, was 160 ng. The minimum immunogenic dose for swine was also 160 ng. The vaccinated swine were challenged with either FMDV A-119 or with heterologous subtype A 24 strain Cruzeiro or type A strain A-CANEFA-1. Those immunized with 640 ng of antigen were about equally immune to the three challenge viruses; most swine having a mouse PD 50 value of 2.0 or greater were immune regardless of which strain was used for challenge. In steers, the smallest dose tested, 40 ng, was satisfactory in eliciting circulating antibodies and immunity. Physical and biological tests indicated that the antigen used in the vaccine is stable for at least 9 months at 4 C.

Antigenicity

Heterologous

10.1128/am.20.5.770-774.1970

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Citations (14)

Animal picornaviruses with a single major species of capsid protein

Biochemical and Biophysical Research Communications (1973)

Howard L. Bachrach W. R. Hess

Picornavirus

Rhinovirus

10.1016/s0006-291x(73)80070-1

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Citations (39)

Analysis by electron microscopy and infectivity of foot-and-mouth disease virus in moving-boundary and zone ultracentrifugation

Archives of Biochemistry and Biophysics (1960)

S. S. Breese Rodes Trautman Howard L. Bachrach

Infectivity

Sedimentation

Analytical Ultracentrifugation

Particle (ecology)

10.1016/0003-9861(60)90115-6

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Citations (8)

Immunobiology of Proteins and Peptides IV: T-Cell Recognition and Antigen Presentation

Howard L. Bachrach

Presentation (obstetrics)

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Citations (0)

Number and Molecular Weights of Foot-and-Mouth Disease Virus Capsid Proteins and the Effects of Maleylation

Journal of Virology (1971)

George F. Vande Woude Howard L. Bachrach

Evidence was obtained by gel electrophoresis that foot-and-mouth disease virus (FMDV) type A(12) protein migrates mainly in a zone corresponding to polypeptide(s) approximately 25,000 daltons in molecular weight. Additional minor components were observed, four with molecular weights ranging from 10,000 to 22,500 daltons and one with a molecular weight of 37,500 daltons. The minor components comprised about 10% of the total protein and were present in variable amounts. The 75S empty capsids contained primarily 25,000-, 37,500- and 50,000-dalton zones. These molecular weights were estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate versus proteins of known molecular weight, including poliovirus and vesicular stomatitis virus proteins. Maleylation of the amino residues of FMDV protein solubilized it to about 5 to 10 mg/ml in aqueous, nondenaturing solvents. This permitted molecular weights to be estimated also by gel filtration. Maleylation of 70% of the available amino groups of the FMDV protein produced heat and sodium dodecyl sulfate-stable polymeric aggregates of 10 to 20% of the 25,000-dalton zone. It also resulted in an increase in the molecular weight of this zone by an amount equivalent (ca. 1,000) to that expected from the added maleyl residues.

Molecular mass

Sodium dodecyl sulfate

10.1128/jvi.7.2.250-259.1971

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Citations (16)