Transfusion transmission of retroviruses: human T‐lymphotropic virus types I and II compared with human immunodeficiency virus type 1

Donegan, Elizabeth; Lee, H; Operskalski, Eva A.; Shaw, GM; Kleinman, Steven; Busch, Michael P.; Stevens, Cladd E.; Schiff, Eugene R.; Nowicki, Marek; Hollingsworth, Charles G.

doi:10.1046/j.1537-2995.1994.34694295061.x

Cited by 130 publications

(98 citation statements)

References 30 publications

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“…The transmission rate of HTLV-I/II ranges from 13-28% in transfusion of HTLV infected red cell /whole blood products with shelf life of 14 days, which increases to 25-75% in transfusion of HTLV infected platelets or cellular products of less than six days [5,6]. The mean utilisation of blood units was 13 days.…”

Section: Discussionmentioning

confidence: 99%

“…The life long risk of developing ATL is 2-5%, while of HAM is 4% in HTLV-I infected individuals [3,4]. Studies have shown transmission efficiency of 13-75 % in recipients of HTLV-I/II infected cellular blood products, which depends on shelf life of cellular blood components [5,6]. Highest HTLV transmission rate of 25-75% is reported in transfusion of cellular blood component in the first five days of shelf life [5,6].…”

Section: H Uman T Cell Leukaemia Virus Type I (Htlv-i)mentioning

confidence: 99%

“…Studies have shown transmission efficiency of 13-75 % in recipients of HTLV-I/II infected cellular blood products, which depends on shelf life of cellular blood components [5,6]. Highest HTLV transmission rate of 25-75% is reported in transfusion of cellular blood component in the first five days of shelf life [5,6]. Shorter incubation and rapid disease progression has been reported in transfusion transmitted HTLV infection due to immuno-suppression in transfusion recipients and neonatal blood transfusion [7,8].…”

Section: H Uman T Cell Leukaemia Virus Type I (Htlv-i)mentioning

confidence: 99%

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Prevalence of Human T Cell Leukaemia Virus amongst Blood Donors

Chaudhari

Shah

Misra³

2009

Medical Journal Armed Forces India

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Section: Discussionmentioning

confidence: 99%

Section: H Uman T Cell Leukaemia Virus Type I (Htlv-i)mentioning

confidence: 99%

Section: H Uman T Cell Leukaemia Virus Type I (Htlv-i)mentioning

confidence: 99%

See 1 more Smart Citation

Prevalence of Human T Cell Leukaemia Virus amongst Blood Donors

Chaudhari

Shah

Misra³

2009

Medical Journal Armed Forces India

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“…The SU-TM oligomeric complex is incorporated into budding virions at the plasma membrane. Unlike other retroviruses, cell-free HTLV-1 virions have very low infectivity (Fan et al, 1992); viral spread is, therefore, likely to occur via Env-mediated fusion between infected cells and target cells (Donegan et al, 1994;Delamarre et al, 1997). Receptor binding is presumed to induce conformational changes in the SU-TM complex that result in TM-mediated fusion between the infected cell and target cell membranes (reviewed in Delamarre et al, 1996).…”

mentioning

confidence: 99%

Crystallization of a trimeric human T cell leukemia virus type 1 gp21 ectodomain fragment as a chimera with maltose‐binding protein

et al. 1998

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We present a novel protein crystallization strategy, applied to the crystallization of human T cell leukemia virus type I (HTLV-I) transmembrane protein gp21 lacking the fusion peptide and the transmembrane domain, as a chimera with the Escherichia coli maltose binding protein (MBP). Crystals could not be obtained with a MBP/gp21 fusion protein in which fusion partners were separated by a flexible linker, but were obtained after connecting the MBP C-terminal a-helix to the predicted N-terminal a-helical sequence of gp21 via three alanine residues. The gp21 sequences conferred a trimeric structure to the soluble fusion proteins as assessed by sedimentation equilibrium and X-ray diffraction, consistent with the trimeric structures of other retroviral transmembrane proteins. The envelope protein precursor, gp62, is likewise trimeric when expressed in mammalian cells. Our results suggest that MBP may have a general application for the crystallization of proteins containing N-terminal a-helical sequences.Keywords: E. coli protein expression; maltose-binding protein/HTLV-1 gp2 1 chimera; protein crystallization; trimerization; X-ray diffraction Crystallization and phase determination remain the two ratelimiting steps in determining protein crystal structures. The strategy of using fusion proteins comprising a "crystallization tag" of known three-dimensional structure and the protein of interest offers an approach to overcoming these problems. The crystallization conditions and crystal contacts found important in crystallization of the tag may be used to guide the crystallization of the fusion protein. Knowledge of the three-dimensional structure of the crystallization tag should then allow determination of the starting phases by the method of molecular replacement. Moreover, knowledge of the heavy atom-binding sites in the crystallization tag can be used to determine the starting phases by the methods of multiple isomorphous replacement and multi-wavelength anomalous dispersion. The strategy offers similar advantages as co-crystallization with antibody fragments (Air et al., 1987;Prongay et al., 1990;Jacobo-Molina et al., 1991;Ostermeier et al., 1995) while being

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“…Ce modèle, applicable à nombre de virus étudiés en laboratoire, fut néanmoins battu en brèche par différentes observations : (1) la transmission in vivo ou in vitro de certains virus nécessite l'inoculation de fractions biologiques contenant des cellules ; (2) l'isolement de particules virales à partir de fluides biologiques ou de surnageants de culture s'avère parfois impossible. Ainsi, il apparaît clairement que pour certains virus comme HTLV-1 (virus de la leucémie humaine à cellules T) [10], peu ou pas de virions « libres » sont relargués par les cellules infectées et que des contacts « physiques » entre cellule infectée et cellule cible sont nécessaires à la transmission des virus [1]. Ce type de dissémination virale mettant en jeu des contacts intercellulaires a soulevé de nombreuses questions : le virus utilise-il des jonctions intercellulaires pré-existantes, les modifie-t-il ou induit-il la formation de nouvelles structures intercellulaires ?…”

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