About: Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection

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About: Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection
Creator	Paciga, Mark Schwartzkopff, Franziska Broder, Christopher Clouse, Kathleen Lankford, Carla Stantchev, Tzanko
Source	Medline; PMC
abstract	BACKGROUND: The role of disulfide bond remodeling in HIV-1 infection is well described, but the process still remains incompletely characterized. At present, the data have been predominantly obtained using established cell lines and/or CXCR4-tropic laboratory-adapted virus strains. There is also ambiguity about which disulfide isomerases/ reductases play a major role in HIV-1 entry, as protein disulfide isomerase (PDI) and/or thioredoxin (Trx) have emerged as the two enzymes most often implicated in this process. RESULTS: We have extended our previous findings and those of others by focusing on CCR5-using HIV-1 strains and their natural targets - primary human macrophages and CD4(+) T lymphocytes. We found that the nonspecific thiol/disulfide exchange inhibitor, 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), significantly reduced HIV-1 entry and infection in cell lines, human monocyte-derived macrophages (MDM), and also phytohemagglutinin (PHA)-stimulated peripheral blood mononuclear cells (PBMC). Subsequent studies were performed using specific anti-PDI or Trx monoclonal antibodies (mAb) in HIV-1 envelope pseudotyped and wild type (wt) virus infection systems. Although human donor-to-donor variability was observed as expected, Trx appeared to play a greater role than PDI in HIV-1 infection of MDM. In contrast, PDI, but not Trx, was predominantly involved in HIV-1 entry and infection of the CD4(+)/CCR5(+) T cell line, PM-1, and PHA-stimulated primary human T lymphocytes. Intriguingly, both PDI and Trx were present on the surface of MDM, PM-1 and PHA-stimulated CD4(+) T cells. However, considerably lower levels of Trx were detected on freshly isolated CD4(+) lymphocytes, compared to PHA-stimulated cells. CONCLUSIONS: Our findings clearly demonstrate the role of thiol/disulfide exchange in HIV-1 entry in primary T lymphocytes and MDM. They also establish a cell-type specificity regarding the involvement of particular disulfide isomerases/reductases in this process and may provide an explanation for differences among previously published studies. More importantly, from an in vivo perspective, the preferential utilization of PDI may be relevant to the HIV-1 entry and establishment of virus reservoirs in resting CD4(+) cells, while the elevated levels of Trx reported in the chronic stages of HIV-1 infection may facilitate the virus entry in macrophages and help to sustain high viremia during the decline of T lymphocytes.
has issue date	2012-12-03(xsd:dateTime)
bibo:doi	10.1186/1742-4690-9-97
bibo:pmid	23206338
has license	cc-by
sha1sum (hex)	209fd978d66d8ffe04712de07dc7e07b779baa08
schema:url	https://doi.org/10.1186/1742-4690-9-97
resource representing a document's title	Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection
has PubMed Central identifier	PMC3526565
has PubMed identifier	23206338
schema:publication	Retrovirology
resource representing a document's body	covid:209fd978d66d8ffe04712de07dc7e07b779baa08#body_text
is schema:about of	named entity 'infection' named entity 'EXCHANGE' named entity 'THIOREDOXIN' named entity 'CELL' named entity 'TYPE' named entity 'HIV-1' named entity 'HAVE' named entity 'STRAINS' named entity 'DESCRIBED' named entity 'REMODELING' named entity 'SPECIFIC' named entity 'HIV-1' named entity 'ROLE' named entity 'ABOUT' named entity 'PROCESS' named entity 'ISOMERASES' named entity 'DATA' named entity 'USING' named entity 'AMBIGUITY' named entity 'TROPIC' named entity 'ESTABLISHED' named entity 'CHARACTERIZED' named entity 'OBTAINED' named entity 'ADAPTED' named entity 'DISULFIDE' named entity 'CXCR4' named entity 'BACKGROUND' named entity 'A MAJOR' named entity 'REQUIREMENTS' named entity 'ENTRY' named entity 'ENZYMES' named entity 'DISULFIDE BOND' named entity 'BUT' named entity 'HIV-1 INFECTION' named entity 'ENTRY' named entity 'LABORATORY' named entity 'PLAY' named entity 'INFECTION' named entity 'THIOL' named entity 'VIRUS' named entity 'PROTEIN DISULFIDE ISOMERASE' named entity 'PRESENT' named entity 'CELL LINES' covid:arg/209fd978d66d8ffe04712de07dc7e07b779baa08 named entity 'virus' named entity 'emerged' named entity 'thioredoxin' named entity 'CXCR4' named entity 'PDI' named entity 'thioredoxin' named entity 'Cell-type' named entity 'infection' named entity 'cell lines' named entity 'clone' named entity 'Env' named entity 'plasmids' named entity 'CCR5' named entity 'clones' named entity 'extracellular' named entity 'cell-type' named entity 'coreceptor' named entity 'APC' named entity 'disulfide exchange' named entity 'Env' named entity 'Trx' named entity 'mAbs' named entity 'gp120' named entity 'Trx' named entity 'amino-terminus' named entity 'interact' named entity 'coiled-coil structure' named entity 'Trx' named entity 'liquid nitrogen' named entity 'HIV-1 infection' named entity 'macrophages' named entity 'HIV-1'

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