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Your search keyword '"Sodroski, Joseph"' showing total 13 results
Start Over Author "Sodroski, Joseph" Journal journal of biological chemistry
13 results on '"Sodroski, Joseph"'

6. Exploring the Stereochemistry of CXCR4-Peptide Recognition and Inhibiting HIV-1 Entry with d-Peptides Derived from Chemokines

Author

Zhou, Naiming, primary, Luo, Zhaowen, additional, Luo, Jiansong, additional, Fan, Xuejun, additional, Cayabyab, Mark, additional, Hiraoka, Megumi, additional, Liu, Dongxiang, additional, Han, Xiaobing, additional, Pesavento, James, additional, Dong, Chang-Zhi, additional, Wang, Youli, additional, An, Jing, additional, Kaji, Hideko, additional, Sodroski, Joseph G., additional, and Huang, Ziwei, additional

Published
2002
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12. Stimulation of enveloped virus infection by beta-amyloid fibrils.

Author

Wojtowicz, Woj M, Farzan, Michael, Joyal, John L, Carter, Kara, Babcock, Gregory J, Israel, David I, Sodroski, Joseph, and Mirzabekov, Tajib

Abstract

Alzheimer's disease is characterized by deposition of beta-amyloid peptide (Abeta) into plaques in the brain, leading to neuronal toxicity and dementia. Human immunodeficiency virus type 1 (HIV-1) infection of the central nervous system can also cause a dementia, and amyloid deposition in the central nervous system is significantly higher in HIV-1-infected individuals compared with uninfected controls. Here we report that Abeta fibrils stimulated, by 5-20-fold, infection of target cells expressing CD4 and an appropriate coreceptor by multiple HIV-1 isolates but did not permit infection of cells lacking these receptors. Abeta enhanced infection at the stage of virus attachment or entry into the cell. Abeta fibrils also stimulated infection by amphotrophic Moloney leukemia virus, herpes simplex virus, and viruses pseudotyped with the envelope glycoprotein of vesicular stomatitis virus. Other synthetic fibril-forming peptides similarly enhanced viral infection and may be useful in gene delivery applications utilizing retroviral vectors. These data suggest that Abeta deposition may increase the vulnerability of the central nervous system to enveloped viral infection and that amyloidogenic peptides could be useful in enhancing gene transfer by enveloped viral vectors.

Published
2002
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13. Determinants of the Higher Order Association of the Restriction Factor TRIM5α and Other Tripartite Motif (TRIM) Proteins.

Author

Xing Li, Yeung, Darwin F., Fiegen, Ann M., and Sodroski, Joseph

Subjects
*DNA restriction enzymes, *RETROVIRUSES, *RETROVIRUS diseases, *OLIGOMERS, *GENETIC mutation
Abstract

Many tripartite motif (TRIM) proteins self-associate, forming dimers and higher order complexes. For example, dimers of TRIM5α, a host factor that restricts retrovirus infection, assemble into higher order arrays on the surface of the viral capsid, resulting in an increase in avidity. Here we show that the higher order association of different TRIM proteins exhibits a wide range of efficiencies. Homologous association (self-association) was more efficient than the heterologous association of different TRIM proteins, indicating that specificity determinants of higher order self-association exist. To investigate the structural determinants of higher order self-association, we studied TRIM mutants and chimeras. These studies revealed the following: 1) the RING domain contributes to the efficiency of higher order self-association, which enhances the binding of TRIM5a to the human immunodeficiency virus (HIV-1) capsid; 2) the RING and B-box 2 domains work together as a homologous unit to promote higher order association of dimers; 3) dimerization is probably required for efficient higher order self-association; 4) the Linker 2 region contributes to higher order self-association, independently of effects of Linker 2 changes on TRIM dimerization; and 5) for efficiently self-associating TRIM proteins, the B30.2(SPRY) domain is not required for higher order self-association. These results support a model in which both ends of the core TRIM dimer (RING-B-box 2 at one end and Linker 2 at the other) contribute to the formation of higher order arrays. [ABSTRACT FROM AUTHOR]

Published
2011
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