HeLp, a heme-transporting lipoprotein with an antioxidant role

Maya‐Monteiro, Clarissa M.; Alves, Liliane R.; Pinhal, Nelson M.; Abdalla, Dulcinéia Saes Parra; Oliveira, Pedro L.

doi:10.1016/j.ibmb.2003.09.005

Cited by 37 publications

(31 citation statements)

References 45 publications

(50 reference statements)

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“…4 The possibility of a function as a source of heme is also supported by the observation that sMF6p/FhHDM-1 binds hemin with medium affinity (K d ϭ 1.14 ϫ 10 Ϫ6 M Ϫ1 ), although the value depends on the redox state of iron and the characteristics of the medium, among other factors. A similar interaction has been reported for other proteins, such as alkyl hydroperoxide reductase (AhpC), belonging to the heme auxotroph Streptococcus agalactiae (42), and HeLp of R. microplus (51), which also inhibit peroxidation of hemin. In addition, sMF6p/FhHDM-1 was also able to inhibit in vitro hemin reactivity to a large extent, which may be important for protecting the cellular environment from hemin toxicity.…”

Section: Discussionsupporting

confidence: 75%

“…In support of this hypothesis, inhibition of hemin degradation and peroxidative activity are both also exhibited by hemopexin. This protein, which is present in vertebrates, has been attributed an antioxidant role against free heme in plasma, and similarly, HeLp and RHBP are able to prevent lipid peroxidation or free radical formation by hemin (16,51).…”

Section: Discussionmentioning

confidence: 99%

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The MF6p/FhHDM-1 Major Antigen Secreted by the Trematode Parasite Fasciola hepatica Is a Heme-binding Protein

Martínez-Sernández

Mezo²,

González-Warleta³

et al. 2014

Journal of Biological Chemistry

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Background:The mechanisms involved in heme handling in trematodes are poorly understood. Results: The biochemical and functional characteristics of a new family of small proteins (MF6p/FhHDM-1) secreted by Fasciola and other trematodes are reported. Conclusion:The Fasciola MF6p/FhHDM-1 major antigen is a heme-binding protein. Significance:Our results provide new insights into the biology of hematophagous trematodes.

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Section: Discussionsupporting

confidence: 75%

Section: Discussionmentioning

confidence: 99%

The MF6p/FhHDM-1 Major Antigen Secreted by the Trematode Parasite Fasciola hepatica Is a Heme-binding Protein

Martínez-Sernández

Mezo²,

González-Warleta³

et al. 2014

Journal of Biological Chemistry

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“…Whether or not this is unique to I. scapularis or that iron-binding proteins were injected at below detectable levels needs further investigation. Published evidence has suggested that the tick may detoxify heme/iron through sequestration in digestive cells (hemosomes) [118,119] and hemolymph [120][121][122]. Data in this study and others [40,41,50,52,123] that show secretion of heme binding proteins in tick saliva suggest a third possibility of eliminating heme through tick saliva.…”

Section: Heme-binding Proteinssupporting

confidence: 50%

Ixodes scapularistick saliva proteins sequentially secreted every 24h during blood feeding

Kim¹

2016

2016 International Congress of Entomology

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Ixodes scapularis is the most medically important tick species and transmits five of the 14 reportable human tick borne disease (TBD) agents in the USA. This study describes LC-MS/MS identification of 582 tick-and 83 rabbit proteins in saliva of I. scapularis ticks that fed for 24,48,72,96, and 120 h, as well as engorged but not detached (BD), and spontaneously detached (SD). The 582 tick proteins include proteases (5.7%), protease inhibitors (7.4%), unknown function proteins (22%), immunity/antimicrobial (2.6%), lipocalin (3.1%), heme/iron binding (2.6%), extracellular matrix/ cell adhesion (2.2%), oxidant metabolism/ detoxification (6%), transporter/ receptor related (3.2%), cytoskeletal (5.5%), and housekeeping-like (39.7%). Notable observations include: (i) tick saliva proteins of unknown function accounting for >33% of total protein content, (ii) 79% of proteases are metalloproteases, (iii) 13% (76/582) of proteins in this study were found in saliva of other tick species and, (iv) ticks apparently selectively inject functionally similar but unique proteins every 24 h, which we speculate is the tick's antigenic variation equivalent strategy to protect important tick feeding functions from host immune system. The host immune responses to proteins present in 24 h I. scapularis saliva will not be effective at later feeding stages. Rabbit proteins identified in our study suggest the tick's strategic use of host proteins to modulate the feeding site. Notably fibrinogen, which is central to blood clotting and wound healing, was detected in high abundance in BD and SD saliva, when the tick is preparing to terminate feeding and detach from the host. A remarkable tick adaptation is that the feeding lesion is completely healed when the tick detaches from the host. Does the tick concentrate fibrinogen at the feeding site to aide in promoting healing of the feeding lesion? Overall, these data provide broad insight into molecular mechanisms regulating different tick feeding phases. These data set the foundation for in depth I. scapularis tick feeding physiology and TBD transmission studies.PLOS Neglected Tropical Diseases |

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“…The success of T. cruzi and of Triatomine spp. depends on the availability of [Fe ++ ] in its environment, as limiting heme availability inhibits reproduction (PaivaSilva et al 2002, Maya-Monteiro et al 2004, and, therefore successful adaptation resulted from this biochemical requirement of both partners. Among the hematophagous bugs belonging to the Family Reduviidae are the strictly hematophagous insects of the Subfamily Triatominae that became adapted to terrestrial ecoregions limited by parallels 42º in the Northern United States and 42º in Southern Argentina.…”

Section: Eons and Interplaymentioning

confidence: 99%