Failure to detect Trichinella spiralis p43 in isolated host nuclei and in irradiated larvae of infected muscle cells which express the infected cell phenotype

Jasmer, Douglas P.; Yao, Sufang; Vassilatis, Demetris K.; Despommier, Dickson D.; Neary, Susan M.

doi:10.1016/0166-6851(94)00131-6

Cited by 24 publications

(9 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This MAb is specific to a tyvelosecontaining glycan determinant synthesized by T. spiralis (1,8,21). Antideglycosylated p43 antibodies (␣-DG p43; IgG and IgA; kindly provided by Dickson Despommier) are rabbit antibodies raised against the p43 T. spiralis stichocyte protein as previously characterized (6,14). The nuclear binding characteristics of and the NA recognized by MAb 9D4 and ␣-DG p43 are indistinguishable (27).…”

Section: Methodsmentioning

confidence: 99%

“…T. spiralis-infected muscle cells, infiltrating cells associated with infected cells, and nuclei from these sources were isolated from mice harboring chronic T. spiralis infections as previously described (12,14). The methods used for indirect immunofluorescence assays (IFAs) were as described previously (27).…”

Section: Methodsmentioning

confidence: 99%

“…Infected cell nuclear preparations are routinely contaminated by infiltrating cell nuclei, a situation which prevents accurate protein quantitation for infected cell nuclei using whole nuclear lysates. However, these two populations can be visually separated by size, nuclear morphology, DNA content, and binding by anti-NA antibodies (11,14).…”

Section: Binding Of Pol II In Infected Cell Nuclei By Mab 8wg16mentioning

confidence: 99%

“…It was suggested that this enlargement could reflect transcription elevated by the parasite in infected cells (9). For instance, antigens ranging in size from about 71 to 97 kDa were detected in host cell nuclei by antibodies specific to a parasite-encoded glycan determinant (14,26,27). These antigens are referred to as nuclear antigens (NA).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Trichinella spiralis -Infected Muscle Cells: Abundant RNA Polymerase II in Nuclear Speckle Domains Colocalizes with Nuclear Antigens

Yao

Jasmer

2001

Infect Immun

View full text Add to dashboard Cite

Infection of mammalian skeletal muscle cells by Trichinella spiralis causes host nuclei to become polyploid (ca. 4N) and abnormally enlarged. It has been postulated that this enlargement reflects an infection-induced elevation of host transcription. Anthelmintic treatment of T. spiralis-infected rodents with mebendazole (MBZ) causes a reduction in the size of infected cell nuclei and a significant reduction in the total RNA content of individual infected muscle cells. A monoclonal antibody to the large subunit of RNA polymerase II (Pol II) was used here to assess the effects of infection on Pol II levels in isolated infected cell nuclei. Pol II was localized to speckle domains in isolated infected cell nuclei. Similar domains have been previously localized to sites of RNA synthesis or processing. When compared to the levels in nuclei from other, uninfected host cells, speckle-localized Pol II (SL-Pol II) levels were significantly elevated in infected cell nuclei by a mean of 3.9-to 6.8-fold. Nuclear antigens (NA) recognized by antibodies against T. spiralis localized to infected cell nuclei. By use of confocal microscopy, a subpopulation of NA was found colocalized with most speckle domains defined by Pol II. MBZ treatment of chronically infected mice, which depletes NA from infected cell nuclei, caused a significant depletion of SL-Pol II from infected cell nuclei. Control nuclei had a mean of 70% more SL-Pol II than MBZ-treated nuclei. The mean residual level of Pol II in these polyploid nuclei remained elevated by 120% over the level in 2N control nuclei. These observations may indicate two distinct effects of infection on Pol II levels in host cells.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Binding Of Pol II In Infected Cell Nuclei By Mab 8wg16mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Trichinella spiralis -Infected Muscle Cells: Abundant RNA Polymerase II in Nuclear Speckle Domains Colocalizes with Nuclear Antigens

Yao

Jasmer

2001

Infect Immun

View full text Add to dashboard Cite

show abstract

“…Vassilatis et al (1992) reported that the antibodies against the 43-kDa recombinant protein strongly reacted with the nurse cell nuclei and the nematode itself. However, Jasmer et al (1994) reported that antibodies which specifically recognized 43-kDa glycoprotein failed to bind detectably with in situ and isolated host nuclei and nuclear extracts. In addition, immunodominant epitopes of specific 43-kDa glycoprotein of T. spiralis could not be detected in hypertrophic nuclei of injected muscles (Ko et al 1994).…”

Section: The 43-kda Glycoproteinmentioning

confidence: 99%

Functional genes and proteins of Trichinella spp.

Nagano

Takahashi

2008

Parasitol Res

View full text Add to dashboard Cite

Research of Trichinella proteins has been conducted with emphasis on excretory-secretory (E-S) products of muscle larvae because of two reasons. The first is that it has prominent and narrow specific antigenicity, and the second is that it may play some role in nurse cell formation after being secreted into host muscle cells. Proteomic analysis of E-S proteins was further advanced by the aid of new analytical methods such as gene cloning, matrix-assisted laser desorption-ionization time-of-flight mass spectrometry, and expressed sequence tags database analysis. As the research progressed, the interest of researchers moved to identification of function of E-S products, which has shed further light on the intriguing relationships between parasites and hosts. Major constituents of the E-S products include 43-, 53-, and 45-kDa glycoprotein derived from the stichosome. Many proteins were discovered in E-S products after the 43-, 53-, and 45-kDa proteins although the relationships among them remain unclear. Some of the new proteins were partially defined in terms of their function including nuclear antigens, MyoD-like protein, TsJ5 protein, etc. There are better-characterized proteins based on the gene molecular method, which allow easier identification of the function of proteins of interest. Such examples were demonstrated by proteinases, proteinase inhibitors, heat shock proteins, glycosidases, etc.

show abstract

Trichinellaand the Nurse Cell

Guiliano¹,

Oksov

2009

Intracellular Niches of Microbes

View full text Add to dashboard Cite

Failure to detect Trichinella spiralis p43 in isolated host nuclei and in irradiated larvae of infected muscle cells which express the infected cell phenotype

Cited by 24 publications

References 18 publications

Trichinella spiralis -Infected Muscle Cells: Abundant RNA Polymerase II in Nuclear Speckle Domains Colocalizes with Nuclear Antigens

Trichinella spiralis -Infected Muscle Cells: Abundant RNA Polymerase II in Nuclear Speckle Domains Colocalizes with Nuclear Antigens

Functional genes and proteins of Trichinella spp.

Trichinellaand the Nurse Cell

Contact Info

Product

Resources

About